Protein profile

KP13_03194

Phosphinothricin N-acetyltransferase

Genome: KpKP13

Gene: AHE43593.1 pat Structure source: AlphaFold + ColabFold UniProt A0A0H3GVE9

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Amino acids 184

Annotations 1

Features 8

PDB binders 4

Druggability 0.383

Overview

Basic information about this protein and its source genome.

Accession: KP13_03194
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE43593.1 pat
Status: annotated
Amino acids: 184
Structure source: AlphaFold + ColabFold

GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Unknown
ColabFold pLDDT: 94.71

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 0.383

Structure A0A0H3GVE9

Pocket Pocket 5

P2Rank 0.924

Structure A0A0H3GVE9

Pocket Pocket 1

ColabFold model

FPocket 0.628 · Pocket 1

P2Rank 0.931 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 67 / 4744 genomes with a hit

Normalized 0.014

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 GO

Gene Ontology (GO)

GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).

Sequence Features

Domain/signature hits from InterPro and related databases.

8 records

Show feature table

Start	End	DB	Term	Name
64	121	CDD	cd04301	NAT_SF
14	169	Pfam	PF13420	Acetyltransferase (GNAT) domain
9	183	Gene3D	G3DSA:3.40.630.30	-
12	176	ProSiteProfiles	PS51186	Gcn5-related N-acetyltransferase (GNAT) domain profile.
12	176	InterPro	IPR000182	GNAT domain
10	178	PANTHER	PTHR43072	N-ACETYLTRANSFERASE
6	177	SUPERFAMILY	SSF55729	Acyl-CoA N-acyltransferases (Nat)
6	177	InterPro	IPR016181	Acyl-CoA N-acyltransferase

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_A0A0H3GVE9	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_03194	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
5				0.383

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				13.63	0.693
2				5.49	0.262

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				0.628
2				0.429

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	16.51	0.78
2	2.99	0.098
3	2.41	0.065

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.

31 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
AZI	2JLM	Q6FBS8	42.0 Da LogP 0.87 TPSA 58.7	✓ Ro5	Alert	`[N-]=[N+]=[N-]`
BLJ	5WPH	Q88LK7	225.1 Da LogP -0.72 TPSA 100.6	✓ Ro5	✓ Clean	`C[As](=O)(CC[C@@H](C(=O)O)N)O`
FLC	4JXQ	Q92L60	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
PPQ	6M7G	Q88LK7	181.1 Da LogP -0.31 TPSA 100.6	✓ Ro5	✓ Clean	`C[P@](=O)(CC[C@@H](C(=O)O)N)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
ZINC1530428	0.600	323.3 Da LogP -1.30 TPSA 158.8	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@H](C)NC(=O)[C@@H](N)CC[P@](C)(=…`
ZINC5882912	0.600	323.3 Da LogP -1.30 TPSA 158.8	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@H](C)NC(=O)[C@H](N)CC[P@](C)(=O…`
ZINC34275204	0.594	209.2 Da LogP 0.73 TPSA 89.6	✓ Ro5	✓ Clean	`CCO[P@](C)(=O)CC[C@H](N)C(=O)O`
ZINC34275205	0.594	209.2 Da LogP 0.73 TPSA 89.6	✓ Ro5	✓ Clean	`CCO[P@@](C)(=O)CC[C@H](N)C(=O)O`
ZINC34275206	0.594	209.2 Da LogP 0.73 TPSA 89.6	✓ Ro5	✓ Clean	`CCO[P@](C)(=O)CC[C@@H](N)C(=O)O`
ZINC34275207	0.594	209.2 Da LogP 0.73 TPSA 89.6	✓ Ro5	✓ Clean	`CCO[P@@](C)(=O)CC[C@@H](N)C(=O)O`
ZINC20112395	0.581	239.2 Da LogP -0.47 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@H](CC[P@](=O)(O)CCC(=O)O)C(=O)O`
ZINC20112808	0.567	211.2 Da LogP -0.25 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@H](CCCCP(=O)(O)O)C(=O)O`
ZINC2169486	0.567	211.2 Da LogP -0.25 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@@H](CCCCP(=O)(O)O)C(=O)O`
ZINC1856281	0.548	225.2 Da LogP 0.14 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@H](CCCCCP(=O)(O)O)C(=O)O`
ZINC2149821	0.548	239.2 Da LogP 0.53 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@@H](CCCCCCP(=O)(O)O)C(=O)O`
ZINC2149823	0.548	239.2 Da LogP 0.53 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@H](CCCCCCP(=O)(O)O)C(=O)O`
ZINC2516019	0.548	225.2 Da LogP 0.14 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@@H](CCCCCP(=O)(O)O)C(=O)O`
ZINC12887775	0.528	295.3 Da LogP 0.81 TPSA 137.9	✓ Ro5	✓ Clean	`CC(C)C[C@H](C[P@@](=O)(O)CC[C@@H](N)C(=O)O)C(=O…`
ZINC4089897	0.528	295.3 Da LogP 0.81 TPSA 137.9	✓ Ro5	✓ Clean	`CC(C)C[C@@H](C[P@](=O)(O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC4089900	0.528	295.3 Da LogP 0.81 TPSA 137.9	✓ Ro5	✓ Clean	`CC(C)C[C@H](C[P@](=O)(O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC56874837	0.515	223.2 Da LogP -0.13 TPSA 103.7	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC[P@](C)(=O)O)C(=O)O`
ZINC59206975	0.515	223.2 Da LogP -0.13 TPSA 103.7	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC[P@](C)(=O)O)C(=O)O`
ZINC2138388	0.500	271.3 Da LogP 1.30 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](CC[P@@](=O)(O)CCc1ccccc1)C(=O)O`
ZINC2138391	0.500	271.3 Da LogP 1.30 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](CC[P@@](=O)(O)CCc1ccccc1)C(=O)O`
ZINC2139781	0.500	269.2 Da LogP -0.41 TPSA 158.2	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](C(=O)O)P(=O)(O)O)C(=O)O`
ZINC2139783	0.500	269.2 Da LogP -0.41 TPSA 158.2	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](C(=O)O)P(=O)(O)O)C(=O)O`
ZINC2139784	0.500	269.2 Da LogP -0.41 TPSA 158.2	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](C(=O)O)P(=O)(O)O)C(=O)O`
ZINC2139785	0.500	269.2 Da LogP -0.41 TPSA 158.2	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@H](C(=O)O)P(=O)(O)O)C(=O)O`
ZINC3055005	0.500	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	0.500	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	0.500	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)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.