Protein profile

KP13_03767

ATP phosphoribosyltransferase

Genome: KpKP13

Gene: AHE43696.1 hisG Structure source: AlphaFold + ColabFold UniProt A0A0H3H0I5

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Amino acids 299

Annotations 6

Features 24

PDB binders 4

Druggability 0.29

Overview

Basic information about this protein and its source genome.

Accession: KP13_03767
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE43696.1 hisG
Status: annotated
Amino acids: 299
Structure source: AlphaFold + ColabFold

2.4.2.17

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid. GO:0003879 Catalysis of the reaction: 1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. GO:0000287 Binding to a magnesium (Mg) ion. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 71.525
DEG E-value: 1.23e-152
Localization: Cytoplasmic
ColabFold pLDDT: 94.36

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 0.29

Structure A0A0H3H0I5

Pocket Pocket 19

P2Rank 0.271

Structure A0A0H3H0I5

Pocket Pocket 1

ColabFold model

FPocket 0.341 · Pocket 9

P2Rank 0.244 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 168 / 4744 genomes with a hit

Normalized 0.035

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

2.4.2.17

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
GO:0003879 Catalysis of the reaction: 1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
200	298	NCBIfam	TIGR03455	ATP phosphoribosyltransferase, C-terminal domain
200	298	InterPro	IPR013115	Histidine biosynthesis HisG, C-terminal
6	220	CDD	cd13592	PBP2_HisGL2
7	221	Gene3D	G3DSA:3.40.190.10	-
102	191	Gene3D	G3DSA:3.40.190.10	-
104	191	FunFam	G3DSA:3.40.190.10:FF:000008	ATP phosphoribosyltransferase
2	298	PANTHER	PTHR21403	ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE
2	298	InterPro	IPR001348	ATP phosphoribosyltransferase HisG
226	299	FunFam	G3DSA:3.30.70.120:FF:000002	ATP phosphoribosyltransferase
156	177	ProSitePatterns	PS01316	ATP phosphoribosyltransferase signature.
156	177	InterPro	IPR018198	ATP phosphoribosyltransferase, conserved site
226	299	Gene3D	G3DSA:3.30.70.120	-
226	299	InterPro	IPR015867	Nitrogen regulatory protein PII/ATP phosphoribosyltransferase, C-terminal
7	197	NCBIfam	TIGR00070	ATP phosphoribosyltransferase
7	197	InterPro	IPR013820	ATP phosphoribosyltransferase, catalytic domain
54	219	Pfam	PF01634	ATP phosphoribosyltransferase
54	219	InterPro	IPR013820	ATP phosphoribosyltransferase, catalytic domain
226	298	SUPERFAMILY	SSF54913	GlnB-like
226	298	InterPro	IPR011322	Nitrogen regulatory PII-like, alpha/beta
6	299	Hamap	MF_00079	ATP phosphoribosyltransferase [hisG].
6	299	InterPro	IPR020621	ATP phosphoribosyltransferase HisG, long form
223	296	Pfam	PF08029	HisG, C-terminal domain
223	296	InterPro	IPR013115	Histidine biosynthesis HisG, C-terminal
6	224	SUPERFAMILY	SSF53850	Periplasmic binding protein-like II

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_A0A0H3H0I5	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_03767	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
19				0.29
3				0.275

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				2.92	0.094
2				0.94	0.004

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
9				0.341

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				2.93	0.094
2				1.23	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.

54 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
PRT	1Q1K	P60757	719.3 Da LogP -3.60 TPSA 385.5	3 viol.	✓ Clean	`[H]/N=C\1/c2c(n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O…`
TIH	5LHT	P9WMN1	171.2 Da LogP 0.70 TPSA 63.3	✓ Ro5	✓ Clean	`c1cc(sc1)C[C@@H](C(=O)O)N`
TLA	1H3D	P60757	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=O)O)O`
WO4	1Z7M	Q02129	247.8 Da LogP -2.62 TPSA 80.3	✓ Ro5	✓ Clean	`[O-][W](=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
ZINC1671208	0.700	200.2 Da LogP 1.08 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)C(Cc1cccs1)C(=O)O`
ZINC12359024	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC34718738	0.661	444.3 Da LogP -1.04 TPSA 206.6	2 viol.	✓ Clean	`O=P(O)(O)O[P@](=O)(O)OC[C@@H]1O[C@H](n2cnc3c(S)…`
ZINC34718739	0.661	444.3 Da LogP -1.04 TPSA 206.6	2 viol.	✓ Clean	`O=P(O)(O)O[P@](=O)(O)OC[C@@H]1O[C@@H](n2cnc3c(S…`
ZINC34718740	0.661	444.3 Da LogP -1.04 TPSA 206.6	2 viol.	✓ Clean	`O=P(O)(O)O[P@](=O)(O)OC[C@@H]1O[C@H](n2cnc3c(S)…`
ZINC34718741	0.661	444.3 Da LogP -1.04 TPSA 206.6	2 viol.	✓ Clean	`O=P(O)(O)O[P@](=O)(O)OC[C@@H]1O[C@@H](n2cnc3c(S…`
ZINC13507175	0.656	451.2 Da LogP -1.08 TPSA 211.0	1 viol.	✓ Clean	`O=P(O)(O)O[P@](=O)(O)OC[C@H]1O[C@@H](n2cnc3c2nc…`
ZINC12360002	0.651	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703	0.651	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599	0.651	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165	0.651	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053	0.651	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433	0.651	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898	0.651	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.651	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020	0.651	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.651	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022	0.651	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC169620381	0.649	261.3 Da LogP 2.36 TPSA 52.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccs1)C(=O)OCc1ccccc1`
ZINC106686432	0.641	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP…`
ZINC12958393	0.641	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)O…`
ZINC35024781	0.641	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC35024785	0.641	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC35024786	0.641	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)…`
ZINC4261903	0.641	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC80601236	0.641	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC95921560	0.641	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC1671214	0.636	238.3 Da LogP 3.22 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)[C@@H](Cc1cccs1)c1cccs1`
ZINC2042523	0.636	238.3 Da LogP 3.22 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)[C@H](Cc1cccs1)c1cccs1`
ZINC17375772	0.621	459.3 Da LogP -1.46 TPSA 232.6	2 viol.	✓ Clean	`Nc1nc(S)c2ncn([C@@H]3O[C@@H](CO[P@](=O)(O)OP(=O…`
ZINC8618621	0.621	459.3 Da LogP -1.46 TPSA 232.6	2 viol.	✓ Clean	`Nc1nc(S)c2ncn([C@H]3O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8618622	0.621	459.3 Da LogP -1.46 TPSA 232.6	2 viol.	✓ Clean	`Nc1nc(S)c2ncn([C@@H]3O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8618623	0.621	459.3 Da LogP -1.46 TPSA 232.6	2 viol.	✓ Clean	`Nc1nc(S)c2ncn([C@H]3O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC37437	0.618	232.3 Da LogP 3.16 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)[C@H](Cc1cccs1)c1ccccc1`
ZINC37438	0.618	232.3 Da LogP 3.16 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)[C@@H](Cc1cccs1)c1ccccc1`
ZINC34619851	0.611	214.2 Da LogP 1.16 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)[C@@H](Cc1cccs1)C(=O)O`
ZINC34619853	0.611	214.2 Da LogP 1.16 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)[C@H](Cc1cccs1)C(=O)O`
ZINC13521831	0.600	492.2 Da LogP -1.21 TPSA 253.1	2 viol.	✓ Clean	`O=P(O)(O)O[P@](=O)(O)O[P@](=O)(O)OC[C@H]1O[C@@H…`
ZINC4419531	0.600	214.2 Da LogP 1.47 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)C[C@H](Cc1cccs1)C(=O)O`
ZINC4419532	0.600	214.2 Da LogP 1.47 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)C[C@@H](Cc1cccs1)C(=O)O`
ZINC33902382	0.597	461.6 Da LogP -1.09 TPSA 232.6	2 viol.	✓ Clean	`Nc1nc(Cl)nc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC33902769	0.597	445.2 Da LogP -1.61 TPSA 232.6	2 viol.	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP…`

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.