Protein target profile

VK055_1174

pyrF

Genome: KpATCC43816 Gene: pyrF AIK79797.1 3D evidence: Experimental + ColabFold model Metabolism 1 reaction UniProt A0A0H3GNE4

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Length 228

Pocket druggability 0.65

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 53 total records

Functional annotation 1 EC 4 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Metabolic bottleneck Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Review the complete evidence below

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: No hit
Gut microbiome similarity: 4.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 85.526 Higher values support similarity to known essential genes.
DEG E-value: 2.71e-141 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 96.04 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

PDB experimental structure

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.65

Structure 8CSO

Pocket Pocket 2

P2Rank 0.688

Structure 8CSO

Pocket Pocket 1

ColabFold model

FPocket 0.529 · Pocket 4

P2Rank 0.734 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 189 / 4744 genomes with a hit

Prevalence 4.0%

Cross-references

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

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a consuming chokepoint reaction in Pyrimidine metabolism, no isoenzyme backup detected, no human homolog detected.

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

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MVALDYDNRDKALAFVDRIDPRDCRLKVGKEMFTLLGPQFVRDLHQRGFEVFLDLKFHDIPNTTARAVAAAAELGVWMVNVHASGGARMMTAAREALLPFGKDAPLLIAVTVLTSMESSDLQDLGITLSPADYAAKLAALTQRCGLDGVVCSAQEAVRFKHELGQAFKLVTPGIRPQGSDAGDQRRIMTPEQAQEAGVDYMVIGRPVTQSADPAATLRAINDSLRKGA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

4.1.1.23

Gene Ontology (GO)

GO:0004590 Catalysis of the reaction: H+ + orotidine 5'-phosphate = CO2 + UMP.
GO:0006207 The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors.
GO:0044205 The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD+ or oxygen.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

18 records

Show feature table

Start	End	DB	Term	Name
2	220	Pfam	PF00215	Orotidine 5'-phosphate decarboxylase / HUMPS family
2	220	InterPro	IPR001754	Orotidine 5'-phosphate decarboxylase domain
1	225	Hamap	MF_01200_B	Orotidine 5'-phosphate decarboxylase [pyrF].
1	225	InterPro	IPR047596	Orotidine 5'-phosphate decarboxylase, bacterial
1	228	FunFam	G3DSA:3.20.20.70:FF:000015	Orotidine 5'-phosphate decarboxylase
1	223	SUPERFAMILY	SSF51366	Ribulose-phoshate binding barrel
1	223	InterPro	IPR011060	Ribulose-phosphate binding barrel
1	220	CDD	cd04725	OMP_decarboxylase_like
1	220	SMART	SM00934	OMPdecase_2
1	220	InterPro	IPR001754	Orotidine 5'-phosphate decarboxylase domain
2	223	PANTHER	PTHR32119	OROTIDINE 5'-PHOSPHATE DECARBOXYLASE
2	223	InterPro	IPR014732	Orotidine 5'-phosphate decarboxylase
51	64	ProSitePatterns	PS00156	Orotidine 5'-phosphate decarboxylase active site.
51	64	InterPro	IPR018089	Orotidine 5'-phosphate decarboxylase, active site
1	228	Gene3D	G3DSA:3.20.20.70	Aldolase class I
1	228	InterPro	IPR013785	Aldolase-type TIM barrel
2	220	NCBIfam	TIGR01740	orotidine-5'-phosphate decarboxylase
2	220	InterPro	IPR014732	Orotidine 5'-phosphate decarboxylase

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 · FPocket

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

Site 1 FPocket #2

0.65

Likely same site as P2Rank 3 2.8 Å 7 shared residues 100% of smaller site

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.688

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Surrounding area

Site 2 P2Rank #2

0.013

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Surrounding area

Site 3 P2Rank #3

0.007

Likely same site as FPocket 2 2.8 Å 7 shared residues 100% of smaller site

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.734

Likely same site as FPocket 1 3.9 Å 14 shared residues 88% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.156

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Surrounding area

Site 3 P2Rank #3

0.034

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Surrounding area

Residue sets

UniProt: Active site:54-54 For OMPdecase activity

UniProt: Active site:56-56 For OMPdecase activity

UniProt: Active site:59-59 For OMPdecase activity

UniProt: Binding site:114-114

UniProt: Binding site:175-175

UniProt: Binding site:184-184

UniProt: Binding site:204-204

UniProt: Binding site:205-205

UniProt: Binding site:27-27

UniProt: Binding site:5-5

UniProt: Binding site:54-63

UniProt: Binding site:59-59

UniProt: Binding site:63-63

All structural evidence 1 experimental · 1 predicted

Structural evidence

1 + 1

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
PDB 8CSO	X-ray	2.60 Å	A,B,C,D,E,F,G,H,I,J	99.6% 2-228	PDBe RCSB PDBj File	Viewing
ColabFold VK055_1174	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.

53 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

BMP PDB via homolog 340.2 Da · LogP -3.03 · TPSA 191.5 Open detail RCSB PDB

BMQ PDB via homolog Detail RCSB PDB

XPE PDB via homolog Detail RCSB PDB

ZINC12501520 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC3870485 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

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
BMP RCSB PDB	1JJK	P08244	340.2 Da LogP -3.03 TPSA 191.5	1 viol.	✓ Clean	`C1=C(N(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
BMQ RCSB PDB	1EIX	P08244	340.2 Da LogP -2.99 TPSA 182.9	✓ Ro5	✓ Clean	`C1C(=O)NC(=O)N(C1=O)[C@H]2[C@@H]([C@@H]([C@H](O…`
XPE RCSB PDB	3UWQ	Q9KQT7	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`C(COCCOCCOCCOCCOCCOCCOCCOCCOCCO)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
ZINC12501520 ZINC	1.000	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC3870485 ZINC	1.000	340.2 Da LogP -2.99 TPSA 182.9	✓ Ro5	✓ Clean	`O=C1CC(=O)N([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3870486 ZINC	1.000	340.2 Da LogP -2.99 TPSA 182.9	✓ Ro5	✓ Clean	`O=C1CC(=O)N([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC3870487 ZINC	1.000	340.2 Da LogP -2.99 TPSA 182.9	✓ Ro5	✓ Clean	`O=C1CC(=O)N([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3870488 ZINC	1.000	340.2 Da LogP -2.99 TPSA 182.9	✓ Ro5	✓ Clean	`O=C1CC(=O)N([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC3874716 ZINC	1.000	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769 ZINC	1.000	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	1.000	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829 ZINC	1.000	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	1.000	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC100351015 ZINC	0.745	368.2 Da LogP -3.04 TPSA 208.6	1 viol.	✓ Clean	`O=C(O)c1cc(=O)[nH]c(=O)n1[C@@H]1O[C@H](COP(=O)(…`
ZINC4095542 ZINC	0.745	368.2 Da LogP -3.04 TPSA 208.6	1 viol.	✓ Clean	`O=C(O)c1cc(=O)[nH]c(=O)n1[C@@H]1O[C@H](COP(=O)(…`
ZINC115086873 ZINC	0.688	209.2 Da LogP -1.08 TPSA 83.2	✓ Ro5	✓ Clean	`NOCCOCCOCCOCCO`
ZINC137432264 ZINC	0.688	457.6 Da LogP -0.91 TPSA 129.3	1 viol.	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC146143823 ZINC	0.688	237.3 Da LogP -1.00 TPSA 83.2	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCO`
ZINC1542984442 ZINC	0.688	413.5 Da LogP -0.93 TPSA 120.1	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1565503710 ZINC	0.688	254.3 Da LogP -0.03 TPSA 57.2	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCS`
ZINC1580161 ZINC	0.688	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	0.688	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	0.688	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1857792028 ZINC	0.688	430.6 Da LogP 0.04 TPSA 94.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC1857792057 ZINC	0.688	474.6 Da LogP 0.06 TPSA 103.3	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC230494776 ZINC	0.688	325.4 Da LogP -0.96 TPSA 101.6	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654 ZINC	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC38917157 ZINC	0.688	210.3 Da LogP -0.04 TPSA 47.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCS`
ZINC44076059 ZINC	0.688	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101 ZINC	0.688	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5650743 ZINC	0.688	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC5997860 ZINC	0.688	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC6403917 ZINC	0.688	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC77271182 ZINC	0.688	281.3 Da LogP -0.98 TPSA 92.4	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCO`
ZINC83253921 ZINC	0.688	369.5 Da LogP -0.95 TPSA 110.9	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC90741446 ZINC	0.688	386.5 Da LogP 0.02 TPSA 84.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC90741447 ZINC	0.688	298.4 Da LogP -0.01 TPSA 66.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCS`
ZINC5439332 ZINC	0.667	260.2 Da LogP -3.11 TPSA 136.4	✓ Ro5	✓ Clean	`O=C1CC(=O)N([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)C…`
ZINC5439333 ZINC	0.667	260.2 Da LogP -3.11 TPSA 136.4	✓ Ro5	✓ Clean	`O=C1CC(=O)N([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)…`
ZINC5439335 ZINC	0.667	260.2 Da LogP -3.11 TPSA 136.4	✓ Ro5	✓ Clean	`O=C1CC(=O)N([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)…`
ZINC5439336 ZINC	0.667	260.2 Da LogP -3.11 TPSA 136.4	✓ Ro5	✓ Clean	`O=C1CC(=O)N([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O…`
ZINC12503831 ZINC	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]2…`
ZINC12503833 ZINC	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H]…`
ZINC13512000 ZINC	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC1532538 ZINC	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC2026984 ZINC	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC2123545 ZINC	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC2606131 ZINC	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC36377965 ZINC	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC3870257 ZINC	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC3870258 ZINC	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC3870260 ZINC	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC9235501 ZINC	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H…`

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.

VK055_1174

Strong target candidate with converging metabolic, structural and chemical evidence.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Structure

Pathways

Metabolic context

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence