Protein profile

VK055_2227

pyrroline-5-carboxylate reductase

Genome: KpATCC43816

Gene: AIK80832.1 proC Structure source: AlphaFold + ColabFold UniProt A0A0H3GIZ4

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Amino acids 269

Annotations 5

Features 21

PDB binders 5

Druggability 0.363

Overview

Basic information about this protein and its source genome.

Accession: VK055_2227
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: AIK80832.1 proC
Status: annotated
Amino acids: 269
Structure source: AlphaFold + ColabFold

1.5.1.2

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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 50.575
Human E-value: 9.52e-20
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 89.963
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 96.29

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.363

Structure A0A0H3GIZ4

Pocket Pocket 8

P2Rank 0.252

Structure A0A0H3GIZ4

Pocket Pocket 1

ColabFold model

FPocket 0.645 · Pocket 15

P2Rank 0.224 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 445 / 4744 genomes with a hit

Normalized 0.094

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

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 Features

Domain/signature hits 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; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

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

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
8				0.363
2				0.129
22				0.078
15				0.021

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	6.12	0.252
2	2.0	0.036
3	1.69	0.024

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
1				0.285
22				0.058
13				0.012
20				0.005

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	5.62	0.224
2	1.98	0.035
3	1.86	0.03
4	1.38	0.014
5	1.27	0.011

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

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	6XP0	P32322	143.1 Da LogP -0.31 TPSA 57.6	✓ Ro5	✓ Clean	`C1C[C@H](N(C1)C=O)C(=O)O`
IQ0	6XP3	P32322	114.1 Da LogP 1.26 TPSA 37.3	✓ Ro5	✓ Clean	`C1CCC(C1)C(=O)O`
PRS	6XP2	P32322	133.2 Da LogP -0.27 TPSA 49.3	✓ Ro5	✓ Clean	`C1[C@H](NCS1)C(=O)O`
T2C	6XP1	P32322	133.2 Da LogP -0.27 TPSA 49.3	✓ Ro5	✓ Clean	`C1CS[C@H](N1)C(=O)O`
TFB	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	0.609	225.3 Da LogP 1.50 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)C2CCCC2)CC1`
ZINC154886	0.583	239.3 Da LogP 1.89 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)C2CCCCC2)CC1`
ZINC37561225	0.583	239.3 Da LogP 1.94 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)C1CCC(NC(=O)C2CCCC2)CC1`
ZINC6741121	0.571	211.3 Da LogP 1.96 TPSA 29.5	✓ Ro5	✓ Clean	`O=C([C@@H]1CCCO1)N1CCCCCCC1`
ZINC6741122	0.571	211.3 Da LogP 1.96 TPSA 29.5	✓ Ro5	✓ Clean	`O=C([C@H]1CCCO1)N1CCCCCCC1`
ZINC1697709	0.565	224.3 Da LogP 3.85 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)C1CCC(CC2CCCCC2)CC1`
ZINC70569221	0.565	211.3 Da LogP 1.11 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)C1CN(C(=O)C2CCCCC2)C1`
ZINC108323602	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	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	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	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	0.560	253.3 Da LogP 2.33 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)C1CCC(NC(=O)C2CCCCC2)CC1`
ZINC19225902	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	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	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	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	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	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	0.552	225.3 Da LogP 2.39 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(NC1CCCCCCC1)[C@H]1CCCO1`
ZINC473793	0.552	225.3 Da LogP 2.39 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(NC1CCCCCCC1)[C@@H]1CCCO1`
ZINC476365	0.552	211.3 Da LogP 2.00 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(NC1CCCCCC1)[C@H]1CCCO1`
ZINC476366	0.552	211.3 Da LogP 2.00 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(NC1CCCCCC1)[C@@H]1CCCO1`
ZINC60121565	0.550	240.3 Da LogP 2.52 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)C1CCC2(CC1)CCC(C(=O)O)CC2`
ZINC11891528	0.548	227.3 Da LogP 0.49 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)[C@@H]2CCCO2)CC1`
ZINC11891532	0.548	227.3 Da LogP 0.49 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)[C@H]2CCCO2)CC1`
ZINC153514	0.542	211.3 Da LogP 1.11 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)C2CCC2)CC1`
ZINC757066037	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	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	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	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	0.542	211.3 Da LogP 2.12 TPSA 40.5	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C2CCCCC2)CC1`
ZINC13153664	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	0.536	254.3 Da LogP -1.28 TPSA 82.3	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@@H]1CCCN1)[C@@H]1CCCN1`
ZINC17722834	0.536	256.3 Da LogP -0.42 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@H]1CCCO1)[C@@H]1CCCO1`
ZINC376062	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	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	0.536	254.3 Da LogP -1.28 TPSA 82.3	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@H]1CCCN1)[C@H]1CCCN1`
ZINC5898346	0.536	256.3 Da LogP -0.42 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@H]1CCCO1)[C@H]1CCCO1`
ZINC5898556	0.536	256.3 Da LogP -0.42 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@@H]1CCCO1)[C@@H]1CCCO1`
ZINC8655607	0.536	254.3 Da LogP -1.28 TPSA 82.3	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@H]1CCCN1)[C@@H]1CCCN1`
ZINC37586180	0.531	241.3 Da LogP 1.02 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)CN(C(=O)[C@@H]1CCCO1)C1CCCC1`
ZINC4899613	0.531	212.2 Da LogP -0.19 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1`
ZINC4974454	0.531	212.2 Da LogP -0.19 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCN1C(=O)[C@H]1CCCN1`
ZINC4974455	0.531	212.2 Da LogP -0.19 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCN1C(=O)[C@@H]1CCCN1`
ZINC4974456	0.531	212.2 Da LogP -0.19 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1C(=O)[C@H]1CCCN1`
ZINC757216905	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	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	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	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	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.