KpATCC43816 Protein target profile

pyrroline-5-carboxylate reductase

Accession: VK055_2227

Gene: AIK80832.1 proC 3D evidence: AlphaFold DB model + ColabFold model Metabolism 4 reactions UniProt A0A0H3GIZ4

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Length 269

Pocket druggability (P2Rank · AlphaFold DB model) 0.252

Metabolic reactions 4

Chokepoint No

Direct ligand evidence 0 55 total records

Functional annotation 1 EC 4 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 5 structural and 0 bioactivity records.

Risks to review

Evidence coverage

Core evidence streams are available for this target.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Human identity (%): 50.575 Lower values reduce human off-target concern.
Human E-value: 9.52e-20
Gut microbiome similarity: 9.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 89.963 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 96.29 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.252

Structure A0A0H3GIZ4

Pocket Pocket 1

Druggability (FPocket) 0.363

Structure A0A0H3GIZ4

Pocket Pocket 8

ColabFold model

P2Rank 0.224 · Pocket 1

FPocket 0.645 · Pocket 15

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 445 / 4744 genomes with a hit

Prevalence 9.4%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MDKKIGFIGCGNMGKAILGGLIASGQVQPGQIWVYTPSPDKVAALRDQYGINAASSAQEVAQIADIVFGAVKPGIMTKVLGDIASSLNKESLVVSIAAGVTLEQLARALGHDRKIIRAMPNTPSLVNAGMTSVTPNALVSSEDVAEVLTIFRCFGQAEQIAEPMIHPVVGVSGSAPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEAVRVLEEKGFRSAVIEAITQCMEKSEKLSRS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

1.5.1.2

Gene Ontology (GO)

GO:0004735 Catalysis of the reaction: L-proline + NADP+ = 1-pyrroline-5-carboxylate + NADPH + H+.
GO:0006561 OBSOLETE. The chemical reactions and pathways resulting in the formation of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0055129 The chemical reactions and pathways resulting in the formation of L-proline, an L-enantiomer of a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

21 records

Show feature table

Start	End	DB	Term	Name
162	268	SUPERFAMILY	SSF48179	6-phosphogluconate dehydrogenase C-terminal domain-like
162	268	InterPro	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
3	266	Hamap	MF_01925	Pyrroline-5-carboxylate reductase [proC].
3	266	InterPro	IPR000304	Pyrroline-5-carboxylate reductase
2	269	PIRSF	PIRSF000193	P5CR
2	269	InterPro	IPR000304	Pyrroline-5-carboxylate reductase
3	268	PANTHER	PTHR11645	PYRROLINE-5-CARBOXYLATE REDUCTASE
165	269	FunFam	G3DSA:1.10.3730.10:FF:000001	Pyrroline-5-carboxylate reductase
4	99	Pfam	PF03807	NADP oxidoreductase coenzyme F420-dependent
4	99	InterPro	IPR028939	Pyrroline-5-carboxylate reductase, catalytic, N-terminal
1	164	FunFam	G3DSA:3.40.50.720:FF:000105	Pyrroline-5-carboxylate reductase
1	158	Gene3D	G3DSA:3.40.50.720	-
222	244	ProSitePatterns	PS00521	Delta 1-pyrroline-5-carboxylate reductase signature.
222	244	InterPro	IPR000304	Pyrroline-5-carboxylate reductase
163	266	Pfam	PF14748	Pyrroline-5-carboxylate reductase dimerisation
163	266	InterPro	IPR029036	Pyrroline-5-carboxylate reductase, dimerisation domain
161	269	Gene3D	G3DSA:1.10.3730.10	-
3	157	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
3	157	InterPro	IPR036291	NAD(P)-binding domain superfamily
5	266	NCBIfam	TIGR00112	pyrroline-5-carboxylate reductase
5	266	InterPro	IPR000304	Pyrroline-5-carboxylate reductase

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.252

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Surrounding area

Pocket 2 P2Rank #2

0.036

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Surrounding area

Pocket 3 P2Rank #3

0.024

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #8

0.363 Unusual size

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Surrounding area

Residue sets

UniProt: Binding site:36-36

UniProt: Binding site:70-73

UniProt: Binding site:8-13

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.224

Likely same site as FPocket 1 5.7 Å 8 shared residues 62% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.035

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Surrounding area

Pocket 3 P2Rank #3

0.03

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Surrounding area

Pocket 4 P2Rank #4

0.014

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Surrounding area

Pocket 5 P2Rank #5

0.011

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #15

0.645

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Surrounding area

Pocket 2 FPocket #1

0.285 Unusual size

Likely same site as P2Rank 1 5.7 Å 8 shared residues 62% of smaller site

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3GIZ4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2227	ColabFold	—	—	full sequence	—	Loaded

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

55 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

FPK PDB via homolog 143.1 Da · LogP -0.31 · TPSA 57.6 Open detail RCSB PDB

IQ0 PDB via homolog Detail RCSB PDB

PRS PDB via homolog Detail RCSB PDB

T2C PDB via homolog Detail RCSB PDB

TFB PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
FPK RCSB PDB	6XP0	P32322	143.1 Da LogP -0.31 TPSA 57.6	✓ Ro5	✓ Clean	`C1C[C@H](N(C1)C=O)C(=O)O`
IQ0 RCSB PDB	6XP3	P32322	114.1 Da LogP 1.26 TPSA 37.3	✓ Ro5	✓ Clean	`C1CCC(C1)C(=O)O`
PRS RCSB PDB	6XP2	P32322	133.2 Da LogP -0.27 TPSA 49.3	✓ Ro5	✓ Clean	`C1[C@H](NCS1)C(=O)O`
T2C RCSB PDB	6XP1	P32322	133.2 Da LogP -0.27 TPSA 49.3	✓ Ro5	✓ Clean	`C1CS[C@H](N1)C(=O)O`
TFB RCSB PDB	5UAV	P32322	116.1 Da LogP 0.25 TPSA 46.5	✓ Ro5	✓ Clean	`C1C[C@H](OC1)C(=O)O`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC13167037 ZINC	0.609	225.3 Da LogP 1.50 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)C2CCCC2)CC1`
ZINC154886 ZINC	0.583	239.3 Da LogP 1.89 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)C2CCCCC2)CC1`
ZINC37561225 ZINC	0.583	239.3 Da LogP 1.94 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)C1CCC(NC(=O)C2CCCC2)CC1`
ZINC6741121 ZINC	0.571	211.3 Da LogP 1.96 TPSA 29.5	✓ Ro5	✓ Clean	`O=C([C@@H]1CCCO1)N1CCCCCCC1`
ZINC6741122 ZINC	0.571	211.3 Da LogP 1.96 TPSA 29.5	✓ Ro5	✓ Clean	`O=C([C@H]1CCCO1)N1CCCCCCC1`
ZINC1697709 ZINC	0.565	224.3 Da LogP 3.85 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)C1CCC(CC2CCCCC2)CC1`
ZINC70569221 ZINC	0.565	211.3 Da LogP 1.11 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)C1CN(C(=O)C2CCCCC2)C1`
ZINC108323602 ZINC	0.563	255.3 Da LogP 1.32 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCCC[C@H]1NC(=O)[C@H]1CCCO1`
ZINC157702634 ZINC	0.563	255.3 Da LogP 1.32 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(N[C@@H]1CCCCC[C@H]1C(=O)O)[C@H]1CCCO1`
ZINC94744170 ZINC	0.563	255.3 Da LogP 1.32 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(N[C@@H]1CCCCC[C@@H]1C(=O)O)[C@@H]1CCCO1`
ZINC94744171 ZINC	0.563	255.3 Da LogP 1.32 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(N[C@@H]1CCCCC[C@H]1C(=O)O)[C@@H]1CCCO1`
ZINC1465716 ZINC	0.560	253.3 Da LogP 2.33 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)C1CCC(NC(=O)C2CCCCC2)CC1`
ZINC19225902 ZINC	0.559	237.2 Da LogP 1.18 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1/C=C/C(=O)C(F)(F)F`
ZINC19225905 ZINC	0.559	237.2 Da LogP 1.18 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCN1/C=C/C(=O)C(F)(F)F`
ZINC33620149 ZINC	0.559	237.2 Da LogP 1.18 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1/C=C\C(=O)C(F)(F)F`
ZINC13968104 ZINC	0.556	282.3 Da LogP 0.02 TPSA 59.1	✓ Ro5	✓ Clean	`O=C([C@@H]1CCCO1)N1CCN(C(=O)[C@H]2CCCO2)CC1`
ZINC5898254 ZINC	0.556	282.3 Da LogP 0.02 TPSA 59.1	✓ Ro5	✓ Clean	`O=C([C@H]1CCCO1)N1CCN(C(=O)[C@H]2CCCO2)CC1`
ZINC5898478 ZINC	0.556	282.3 Da LogP 0.02 TPSA 59.1	✓ Ro5	✓ Clean	`O=C([C@@H]1CCCO1)N1CCN(C(=O)[C@@H]2CCCO2)CC1`
ZINC473792 ZINC	0.552	225.3 Da LogP 2.39 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(NC1CCCCCCC1)[C@H]1CCCO1`
ZINC473793 ZINC	0.552	225.3 Da LogP 2.39 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(NC1CCCCCCC1)[C@@H]1CCCO1`
ZINC476365 ZINC	0.552	211.3 Da LogP 2.00 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(NC1CCCCCC1)[C@H]1CCCO1`
ZINC476366 ZINC	0.552	211.3 Da LogP 2.00 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(NC1CCCCCC1)[C@@H]1CCCO1`
ZINC60121565 ZINC	0.550	240.3 Da LogP 2.52 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)C1CCC2(CC1)CCC(C(=O)O)CC2`
ZINC11891528 ZINC	0.548	227.3 Da LogP 0.49 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)[C@@H]2CCCO2)CC1`
ZINC11891532 ZINC	0.548	227.3 Da LogP 0.49 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)[C@H]2CCCO2)CC1`
ZINC153514 ZINC	0.542	211.3 Da LogP 1.11 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)C2CCC2)CC1`
ZINC757066037 ZINC	0.542	200.2 Da LogP 1.44 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CCC[C@@H](C(=O)O)CC1`
ZINC757066044 ZINC	0.542	200.2 Da LogP 1.44 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CCC[C@H](C(=O)O)CC1`
ZINC757066048 ZINC	0.542	200.2 Da LogP 1.44 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)[C@H]1CCC[C@@H](C(=O)O)CC1`
ZINC757066049 ZINC	0.542	200.2 Da LogP 1.44 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)[C@H]1CCC[C@H](C(=O)O)CC1`
ZINC8727458 ZINC	0.542	211.3 Da LogP 2.12 TPSA 40.5	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C2CCCCC2)CC1`
ZINC13153664 ZINC	0.536	310.4 Da LogP 0.89 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(NC1CCC(NC(=O)[C@H]2CCCO2)CC1)[C@@H]1CCCO1`
ZINC1616450 ZINC	0.536	254.3 Da LogP -1.28 TPSA 82.3	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@@H]1CCCN1)[C@@H]1CCCN1`
ZINC17722834 ZINC	0.536	256.3 Da LogP -0.42 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@H]1CCCO1)[C@@H]1CCCO1`
ZINC376062 ZINC	0.536	310.4 Da LogP 0.89 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(NC1CCC(NC(=O)[C@H]2CCCO2)CC1)[C@H]1CCCO1`
ZINC376065 ZINC	0.536	310.4 Da LogP 0.89 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(NC1CCC(NC(=O)[C@@H]2CCCO2)CC1)[C@@H]1CCCO1`
ZINC5600257 ZINC	0.536	254.3 Da LogP -1.28 TPSA 82.3	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@H]1CCCN1)[C@H]1CCCN1`
ZINC5898346 ZINC	0.536	256.3 Da LogP -0.42 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@H]1CCCO1)[C@H]1CCCO1`
ZINC5898556 ZINC	0.536	256.3 Da LogP -0.42 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@@H]1CCCO1)[C@@H]1CCCO1`
ZINC8655607 ZINC	0.536	254.3 Da LogP -1.28 TPSA 82.3	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@H]1CCCN1)[C@@H]1CCCN1`
ZINC37586180 ZINC	0.531	241.3 Da LogP 1.02 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)CN(C(=O)[C@@H]1CCCO1)C1CCCC1`
ZINC4899613 ZINC	0.531	212.2 Da LogP -0.19 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1`
ZINC4974454 ZINC	0.531	212.2 Da LogP -0.19 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCN1C(=O)[C@H]1CCCN1`
ZINC4974455 ZINC	0.531	212.2 Da LogP -0.19 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCN1C(=O)[C@@H]1CCCN1`
ZINC4974456 ZINC	0.531	212.2 Da LogP -0.19 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1C(=O)[C@H]1CCCN1`
ZINC757216905 ZINC	0.531	212.3 Da LogP 0.44 TPSA 61.4	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1C[C@@H]([C@@H]2CCCNC2)CCN1`
ZINC757216906 ZINC	0.531	212.3 Da LogP 0.44 TPSA 61.4	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1C[C@H]([C@@H]2CCCNC2)CCN1`
ZINC757216908 ZINC	0.531	212.3 Da LogP 0.44 TPSA 61.4	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1C[C@@H]([C@H]2CCCNC2)CCN1`
ZINC757216910 ZINC	0.531	212.3 Da LogP 0.44 TPSA 61.4	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1C[C@H]([C@H]2CCCNC2)CCN1`
ZINC14806503 ZINC	0.529	216.2 Da LogP 0.27 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)C1CC(C(=O)O)CC(C(=O)O)C1`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GIZ4

Pathways

BioCyc RXN66-546-4-HYDROXY-L-PROLINE/NADP//PYRROLINE-HYDROXY-CARBOXYLATE/NADPH/PROTON.69. BioCyc RXN66-546-4-HYDROXY-L-PROLINE/NAD//PYRROLINE-HYDROXY-CARBOXYLATE/NADH/PROTON.67. BioCyc PYRROLINECARBREDUCT-RXN-PRO/NADP//L-DELTA1-PYRROLINE_5-CARBOXYLATE/NADPH/PROTON.56. BioCyc PYRROLINECARBREDUCT-RXN-PRO/NAD//L-DELTA1-PYRROLINE_5-CARBOXYLATE/NADH/PROTON.54.