Protein profile

PA3151

imidazole glycerol phosphate synthase subunit HisF

Genome: NC_002516.2

Gene: PA3151 hisF2 Structure source: AlphaFold UniProt P72139

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Amino acids 251

Annotations 6

Features 12

PDB binders 7

Druggability 0.706

Overview

Basic information about this protein and its source genome.

Accession: PA3151
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3151 hisF2
Status: annotated
Amino acids: 251
Structure source: AlphaFold

4.3.2.10

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0000107 Catalysis of the reaction: phosphoribulosylformimino-AICAR-P + L-glutamine = D-erythro-imidazole-glycerol-phosphate + aminoimidazole carboxamide ribonucleotide + L-glutamate + 2 H+. GO:0016833 Catalysis of the cleavage of a C-C bond by other means than by hydrolysis or oxidation, of a 3-hydroxy acid. GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid. GO:0009243 The chemical reactions and pathways resulting in the formation of the O side chain of a lipopolysaccharide, which determines the antigenic specificity of the organism. It is made up of about 50 repeating units of a branched tetrasaccharide.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Cytoplasmic

Selected Druggability evidence

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 0.706

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MVRRRVIPCLLLKDRGLVKTVKFKEPKYVGDPINAIRIFNEKEVDELILLDIDASRLNQEPNYELIAEVAGECFMPICYGGGIKTLEHAEKIFSLGVEKVSINTAALMDLSLIRRIADKFGSQSVVGSIDCRKGFWGGHSVFSENGTRDMKRSPLEWAQALEEAGVGEIFLNSIDRDGVQKGFDNALVENIASNVHVPVIACGGAGSIADLIDLFERTCVSAVAAGSLFVFHGKHRAVLISYPDVNKLDVG

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

4.3.2.10

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0000107 Catalysis of the reaction: phosphoribulosylformimino-AICAR-P + L-glutamine = D-erythro-imidazole-glycerol-phosphate + aminoimidazole carboxamide ribonucleotide + L-glutamate + 2 H+.
GO:0016833 Catalysis of the cleavage of a C-C bond by other means than by hydrolysis or oxidation, of a 3-hydroxy acid.
GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
GO:0009243 The chemical reactions and pathways resulting in the formation of the O side chain of a lipopolysaccharide, which determines the antigenic specificity of the organism. It is made up of about 50 repeating units of a branched tetrasaccharide.

Sequence Features

Domain/signature hits from InterPro and related databases.

12 records

Show feature table

Start	End	DB	Term	Name
4	243	CDD	cd04731	HisF
4	243	InterPro	IPR004651	Histidine biosynthesis, HisF
1	231	NCBIfam	TIGR03572	glycosyl amidation-associated protein WbuZ
1	231	InterPro	IPR020021	Glycosyl amidation-associated protein, WbuZ
1	243	Gene3D	G3DSA:3.20.20.70	Aldolase class I
1	243	InterPro	IPR013785	Aldolase-type TIM barrel
3	248	NCBIfam	NF038364	AglZ/HisF2 family acetamidino modification protein
1	232	SUPERFAMILY	SSF51366	Ribulose-phoshate binding barrel
1	232	InterPro	IPR011060	Ribulose-phosphate binding barrel
2	230	PANTHER	PTHR21235	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H IGP SYNTHASE SUBUNIT HISF/H
5	232	Pfam	PF00977	Histidine biosynthesis protein
5	232	InterPro	IPR006062	Histidine biosynthesis protein

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA3151	AlphaFold	—	—	full sequence	—	Viewing

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
2				0.706

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.

57 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 57 via homologs

Structural ligands 7 0 loaded crystals

Bioactive compounds 0 50 ZINC candidates

Drug-like & clean 41 0 PAINS alerts

Best available ligand signal

0VR PDB via homolog 351.2 Da · LogP -1.01 · TPSA 176.8

0VR PDB via homolog 1PR PDB via homolog 2ER PDB via homolog AMZ PDB via homolog

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
0VR	4EWN	Q9X0C6	351.2 Da LogP -1.01 TPSA 176.8	1 viol.	✓ Clean	`c1ccc(c(c1)C(=O)O)NC[C@@H]([C@@H]([C@@H](COP(=O…`
1PR	1OX5	P33734	581.4 Da LogP -5.14 TPSA 328.9	3 viol.	✓ Clean	`c1nc(c(n1[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)(O…`
2ER	5AB3	P10372	577.3 Da LogP -4.45 TPSA 326.0	3 viol.	✓ Clean	`c1nc(c(n1[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)(O…`
AMZ	5DN1	P16250	338.2 Da LogP -2.71 TPSA 203.4	1 viol.	✓ Clean	`c1nc(c(n1[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)(O…`
CXS	4X2R	C0W7K4	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCCS(=O)(=O)O`
GUO	5A5W	P10372	577.3 Da LogP -4.48 TPSA 318.2	3 viol.	✓ Clean	`c1nc(c(n1[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)(O…`
POP	1JVN	P33734	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=O)(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
ZINC2004372	1.000	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC38364153	0.926	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC1710230	0.786	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC2390999	0.655	275.3 Da LogP -1.99 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC4096530	0.647	366.2 Da LogP -2.72 TPSA 206.5	1 viol.	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC5188799	0.630	280.5 Da LogP 4.39 TPSA 24.1	✓ Ro5	✓ Clean	`C(CCCNC1CCCCC1)CCNC1CCCCC1`
ZINC3055005	0.591	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O`
ZINC3055007	0.591	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055010	0.591	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC2391099	0.586	274.3 Da LogP -2.59 TPSA 178.6	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC103317774	0.582	338.2 Da LogP -2.71 TPSA 203.4	1 viol.	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC12501010	0.582	338.2 Da LogP -2.71 TPSA 203.4	1 viol.	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC22048479	0.582	338.2 Da LogP -2.71 TPSA 203.4	1 viol.	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC3869390	0.582	338.2 Da LogP -2.71 TPSA 203.4	1 viol.	✓ Clean	`NC(=O)c1ncn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869391	0.582	338.2 Da LogP -2.71 TPSA 203.4	1 viol.	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC3869392	0.582	338.2 Da LogP -2.71 TPSA 203.4	1 viol.	✓ Clean	`NC(=O)c1ncn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869393	0.582	338.2 Da LogP -2.71 TPSA 203.4	1 viol.	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC4096500	0.582	338.2 Da LogP -2.71 TPSA 203.4	1 viol.	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC2556600	0.567	217.2 Da LogP -1.83 TPSA 135.5	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@@H](N)CCC(N)=O)C(=O)O`
ZINC1555366	0.565	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1555367	0.565	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1555369	0.565	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720127	0.565	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1720128	0.565	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720130	0.565	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1581634	0.552	203.2 Da LogP -2.22 TPSA 135.5	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](N)C(=O)NCC(=O)O`
ZINC5500823	0.552	203.2 Da LogP -2.22 TPSA 135.5	✓ Ro5	✓ Clean	`NC(=O)CC[C@@H](N)C(=O)NCC(=O)O`
ZINC2509149	0.531	211.4 Da LogP 4.27 TPSA 12.0	✓ Ro5	✓ Clean	`CCCCCCCCNC1CCCCC1`
ZINC2560992	0.531	275.3 Da LogP -1.99 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC130127586	0.529	260.4 Da LogP 1.38 TPSA 58.2	✓ Ro5	✓ Clean	`O=S(=O)(NCCNC1CCCCCC1)C1CC1`
ZINC1703514	0.520	285.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1NC[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC4824070	0.520	285.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1NC[C@H](O)[C@H](O)[C@H](O)CO`
ZINC4824072	0.520	285.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1NC[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC4824074	0.520	285.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1NC[C@@H](O)[C@@H](O)[C@H](O)CO`
ZINC19367005	0.519	224.4 Da LogP 2.83 TPSA 24.1	✓ Ro5	✓ Clean	`C1CCC(NCCNC2CCCCC2)CC1`
ZINC2106542	0.519	245.3 Da LogP 1.99 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCCCCCC(=O)O)C(=O)O`
ZINC2106543	0.519	245.3 Da LogP 1.99 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCCCCCC(=O)O)C(=O)O`
ZINC2108713	0.519	217.3 Da LogP 1.21 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCCCC(=O)O)C(=O)O`
ZINC2108714	0.519	217.3 Da LogP 1.21 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCCCC(=O)O)C(=O)O`
ZINC1529737	0.517	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC1576202	0.517	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)NCC(=O)O)C(=O)O`
ZINC2384790	0.517	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC2560745	0.517	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC2560989	0.517	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC3995565	0.517	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)NCC(=O)O)C(=O)O`
ZINC53683597	0.517	202.3 Da LogP -0.08 TPSA 95.4	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)[C@@H](N)CCC(N)=O`
ZINC56963153	0.517	202.3 Da LogP -0.08 TPSA 95.4	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)[C@H](N)CCC(N)=O`
ZINC4096533	0.514	339.2 Da LogP -2.11 TPSA 197.6	1 viol.	✓ Clean	`Nc1c(C(=O)O)ncn1[C@@H]1O[C@H](COP(=O)(O)O)[C@@H…`
ZINC88466335	0.514	338.2 Da LogP -2.71 TPSA 203.4	1 viol.	✓ Clean	`NC(=O)c1c(N)ncn1[C@@H]1O[C@H](COP(=O)(O)O)[C@@H…`
ZINC2168583	0.500	237.3 Da LogP 0.16 TPSA 86.6	✓ Ro5	✓ Clean	`O=S(=O)(O)C[C@@H](O)CNC1CCCCC1`

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.