Protein profile

KP13_05054

GTP cyclohydrolase 1

Genome: KpKP13

Gene: AHE43573.1 folE Structure source: AlphaFold + ColabFold UniProt A0A0H3GVG9

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Amino acids 222

Annotations 8

Features 19

PDB binders 5

Druggability 0.425

Overview

Basic information about this protein and its source genome.

Accession: KP13_05054
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE43573.1 folE
Status: annotated
Amino acids: 222
Structure source: AlphaFold + ColabFold

3.5.4.16

GO:0003934 Catalysis of the reaction: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H+. GO:0046654 The chemical reactions and pathways resulting in the formation of tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005525 Binding to GTP, guanosine triphosphate. GO:0008270 Binding to a zinc ion (Zn). GO:0006730 The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 36.0
Human E-value: 2.62e-34
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 94.144
DEG E-value: 9.73e-151
Localization: Cytoplasmic
ColabFold pLDDT: 97.03

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 0.425

Structure A0A0H3GVG9

Pocket Pocket 4

P2Rank 0.23

Structure A0A0H3GVG9

Pocket Pocket 1

ColabFold model

FPocket 0.413 · Pocket 2

P2Rank 0.264 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 162 / 4744 genomes with a hit

Normalized 0.034

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

3.5.4.16

Gene Ontology (GO)

GO:0003934 Catalysis of the reaction: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H+.
GO:0046654 The chemical reactions and pathways resulting in the formation of tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005525 Binding to GTP, guanosine triphosphate.
GO:0008270 Binding to a zinc ion (Zn).
GO:0006730 The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
GO:0006729 The chemical reactions and pathways resulting in the formation of tetrahydrobiopterin, the reduced form of biopterin (2-amino-4-hydroxy-6-(1,2-dihydroxypropyl)-pteridine). It functions as a hydroxylation coenzyme, e.g. in the conversion of phenylalanine to tyrosine.

Sequence Features

Domain/signature hits from InterPro and related databases.

19 records

Show feature table

Start	End	DB	Term	Name
98	114	ProSitePatterns	PS00859	GTP cyclohydrolase I signature 1.
98	114	InterPro	IPR018234	GTP cyclohydrolase I, conserved site
146	156	ProSitePatterns	PS00860	GTP cyclohydrolase I signature 2.
146	156	InterPro	IPR018234	GTP cyclohydrolase I, conserved site
40	220	NCBIfam	TIGR00063	GTP cyclohydrolase I FolE
40	220	InterPro	IPR001474	GTP cyclohydrolase I
29	220	PANTHER	PTHR11109	GTP CYCLOHYDROLASE I
29	220	InterPro	IPR001474	GTP cyclohydrolase I
87	222	Gene3D	G3DSA:3.30.1130.10	-
87	222	InterPro	IPR043133	GTP cyclohydrolase I, C-terminal/NADPH-dependent 7-cyano-7-deazaguanine reductase
87	219	FunFam	G3DSA:3.30.1130.10:FF:000001	GTP cyclohydrolase 1
41	218	Pfam	PF01227	GTP cyclohydrolase I
41	218	InterPro	IPR020602	GTP cyclohydrolase I domain
4	221	SUPERFAMILY	SSF55620	Tetrahydrobiopterin biosynthesis enzymes-like
36	219	Hamap	MF_00223	GTP cyclohydrolase 1 [folE].
36	219	InterPro	IPR001474	GTP cyclohydrolase I
2	86	Gene3D	G3DSA:1.10.286.10	-
2	86	InterPro	IPR043134	GTP cyclohydrolase I, N-terminal domain
2	86	FunFam	G3DSA:1.10.286.10:FF:000002	GTP cyclohydrolase 1

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_A0A0H3GVG9	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_05054	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
4				0.425

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	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				2.75	0.083
2				0.99	0.005

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
2				0.413
4				0.272

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	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				2.83	0.088

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
3PO	1WPL	P22288	258.0 Da LogP -0.69 TPSA 170.8	✓ Ro5	✓ Clean	`OP(=O)(O)OP(=O)(O)OP(=O)(O)O`
8DG	1WUR	Q5SH52	523.2 Da LogP -2.01 TPSA 298.8	3 viol.	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C3=C(C(=O)NC(=N3)N)NC2=…`
8GT	6Z80	P30793	539.2 Da LogP -3.04 TPSA 319.1	3 viol.	✓ Clean	`C([C@@H]1[C@H]([C@H]([C@@H](O1)N2C3=C(C(=O)NC(=…`
HBI	1WPL	P22288	239.2 Da LogP -1.41 TPSA 136.6	✓ Ro5	✓ Clean	`C[C@@H]([C@@H](C1=NC2=C(NC1)N=C(NC2=O)N)O)O`
QBK	6Z88	P30793	182.2 Da LogP -0.45 TPSA 97.2	✓ Ro5	✓ Clean	`C12=NC(=O)SC1=NC(=NC2=O)N`

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
ZINC18181336	1.000	239.2 Da LogP -1.41 TPSA 136.6	✓ Ro5	✓ Clean	`C[C@H](O)[C@H](O)C1=Nc2c(nc(N)[nH]c2=O)NC1`
ZINC6827739	1.000	258.0 Da LogP -0.69 TPSA 170.8	✓ Ro5	✓ Clean	`O=P(O)(O)OP(=O)(O)OP(=O)(O)O`
ZINC95617488	1.000	239.2 Da LogP -1.41 TPSA 136.6	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H](O)C1=Nc2c(nc(N)[nH]c2=O)NC1`
ZINC113264413	0.778	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC113264415	0.778	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC2244337	0.778	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC2244338	0.778	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC1834294	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc(C[C@H](N)C(=O)O)c1)C(=O)O`
ZINC1834295	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc(C[C@@H](N)C(=O)O)c1)C(=O)O`
ZINC1834297	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](Cc1cccc(C[C@@H](N)C(=O)O)c1)C(=O)O`
ZINC3869856	0.744	255.2 Da LogP -2.44 TPSA 156.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N=C([C@@H](O)[C@H](O)CO)CN2`
ZINC4096578	0.744	255.2 Da LogP -2.44 TPSA 156.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N=C([C@H](O)[C@H](O)CO)CN2`
ZINC39351856	0.731	328.4 Da LogP 1.26 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1)C…`
ZINC2561081	0.724	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC2561082	0.724	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC12503703	0.708	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(…`
ZINC8215878	0.708	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O…`
ZINC113539705	0.700	265.3 Da LogP 2.04 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C#Cc2ccccc2)cc1)C(=O)O`
ZINC113539708	0.700	265.3 Da LogP 2.04 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C#Cc2ccccc2)cc1)C(=O)O`
ZINC116910786	0.700	269.3 Da LogP 3.06 TPSA 88.0	✓ Ro5	Alert	`N[C@@H](Cc1ccc(/N=N/c2ccccc2)cc1)C(=O)O`
ZINC29566843	0.700	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1cccc(-c2ccccc2)c1)C(=O)O`
ZINC29570997	0.700	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc(-c2ccccc2)c1)C(=O)O`
ZINC44283581	0.700	257.3 Da LogP 2.43 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccccc2)cc1)C(=O)O`
ZINC44283583	0.700	257.3 Da LogP 2.43 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Oc2ccccc2)cc1)C(=O)O`
ZINC2111574	0.692	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1C[C@H](N)C(=O)O)C(=O)O`
ZINC2111575	0.692	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1C[C@@H](N)C(=O)O)C(=O)O`
ZINC2111578	0.692	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccccc1C[C@@H](N)C(=O)O)C(=O)O`
ZINC12648269	0.690	237.3 Da LogP 0.73 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](C[C@@H](Cc1ccccc1)C(=O)O)C(=O)O`
ZINC1616445	0.690	354.5 Da LogP 0.36 TPSA 110.2	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1)C(=O)NCCNC(=O)[C@H](N)Cc1cccc…`
ZINC1616446	0.690	354.5 Da LogP 0.36 TPSA 110.2	✓ Ro5	✓ Clean	`N[C@H](Cc1ccccc1)C(=O)NCCNC(=O)[C@H](N)Cc1ccccc1`
ZINC1616447	0.690	354.5 Da LogP 0.36 TPSA 110.2	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1)C(=O)NCCNC(=O)[C@@H](N)Cc1ccc…`
ZINC5225893	0.690	237.3 Da LogP 0.73 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](C[C@H](Cc1ccccc1)C(=O)O)C(=O)O`
ZINC133159	0.688	271.3 Da LogP 2.22 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(OCc2ccccc2)cc1)C(=O)O`
ZINC133162	0.688	271.3 Da LogP 2.22 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(OCc2ccccc2)cc1)C(=O)O`
ZINC32333	0.679	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC32334	0.679	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC3679925	0.679	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(I)cc1)C(=O)O`
ZINC391104	0.679	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(I)cc1)C(=O)O`
ZINC4202286	0.679	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC4202287	0.679	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC6092920	0.679	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC6506146	0.679	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC6580731	0.679	225.3 Da LogP 2.44 TPSA 43.1	✓ Ro5	✓ Clean	`N[C@H](Cc1ccccc1)C(=O)c1ccccc1`
ZINC90624143	0.679	225.3 Da LogP 2.44 TPSA 43.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1)C(=O)c1ccccc1`
ZINC54918280	0.667	254.3 Da LogP 1.87 TPSA 55.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1)C(=O)NCc1ccccc1`
ZINC54918281	0.667	254.3 Da LogP 1.87 TPSA 55.1	✓ Ro5	✓ Clean	`N[C@H](Cc1ccccc1)C(=O)NCc1ccccc1`
ZINC12504289	0.662	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839	0.662	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491	0.662	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481	0.662	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`

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.