Protein profile

KP13_01289

Aspartate carbamoyltransferase regulatory chain

Genome: KpKP13

Gene: pyrI AHE46645.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GLQ7

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Amino acids 153

Annotations 2

Features 19

PDB binders 2

Druggability 0.787

Overview

Basic information about this protein and its source genome.

Accession: KP13_01289
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: pyrI AHE46645.1
Status: annotated
Amino acids: 153
Structure source: AlphaFold + ColabFold

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:0009347 A multienzyme complex that catalyzes the formation N-carbamoyl-L-aspartate from carbamoyl phosphate and L-aspartate. It exhibits a variety of architectural organizations, but in all microorganisms the core catalytic component is a homotrimer of approximately 34 kDa polypeptides.

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 (%): 62.0
DEG E-value: 1.4599999999999999e-67
Localization: Cytoplasmic
ColabFold pLDDT: 89.69

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 0.787

Structure A0A0H3GLQ7

Pocket Pocket 1

P2Rank 0.035

Structure A0A0H3GLQ7

Pocket Pocket 1

ColabFold model

FPocket 0.284 · Pocket 6

P2Rank 0.086 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 127 / 4744 genomes with a hit

Normalized 0.027

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 GO

Gene Ontology (GO)

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:0009347 A multienzyme complex that catalyzes the formation N-carbamoyl-L-aspartate from carbamoyl phosphate and L-aspartate. It exhibits a variety of architectural organizations, but in all microorganisms the core catalytic component is a homotrimer of approximately 34 kDa polypeptides.

Sequence Features

Domain/signature hits from InterPro and related databases.

19 records

Show feature table

Start	End	DB	Term	Name
2	100	FunFam	G3DSA:3.30.70.140:FF:000001	Aspartate carbamoyltransferase regulatory chain
102	147	Pfam	PF02748	Aspartate carbamoyltransferase regulatory chain, metal binding domain
102	147	InterPro	IPR020542	Aspartate carbamoyltransferase regulatory subunit, C-terminal
102	150	SUPERFAMILY	SSF57825	Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain
102	150	InterPro	IPR036792	Aspartate carbamoyltransferase regulatory subunit, C-terminal domain superfamily
101	153	FunFam	G3DSA:2.30.30.20:FF:000001	Aspartate carbamoyltransferase regulatory chain
4	152	Hamap	MF_00002	Aspartate carbamoyltransferase regulatory chain [pyrI].
4	152	InterPro	IPR002801	Aspartate transcarbamylase regulatory subunit
2	100	SUPERFAMILY	SSF54893	Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain
2	100	InterPro	IPR036793	Aspartate carbamoyltransferase regulatory subunit, N-terminal domain superfamily
101	153	Gene3D	G3DSA:2.30.30.20	-
1	151	PANTHER	PTHR35805	ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN
1	151	InterPro	IPR002801	Aspartate transcarbamylase regulatory subunit
7	96	Pfam	PF01948	Aspartate carbamoyltransferase regulatory chain, allosteric domain
7	96	InterPro	IPR020545	Aspartate carbamoyltransferase regulatory subunit, N-terminal
1	100	Gene3D	G3DSA:3.30.70.140	-
1	100	InterPro	IPR036793	Aspartate carbamoyltransferase regulatory subunit, N-terminal domain superfamily
5	152	NCBIfam	TIGR00240	aspartate carbamoyltransferase regulatory subunit
5	152	InterPro	IPR002801	Aspartate transcarbamylase regulatory subunit

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_A0A0H3GLQ7	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_01289	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
1				0.787

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				1.15	0.009

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
6				0.284

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				1.49	0.021

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.

52 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
DCP	4FYX	P0A7F3	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=CC(=NC2=O)N)CO[P@@](=…`
PAL	1I5O	P0A7F3	255.1 Da LogP -1.79 TPSA 161.2	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)NC(=O)CP(=O)(O)O)C(=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
ZINC12503365	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](CO[P@](=O)(O)O[P@…`
ZINC13435050	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
ZINC1563934	1.000	255.1 Da LogP -1.79 TPSA 161.2	✓ Ro5	✓ Clean	`O=C(O)C[C@H](NC(=O)CP(=O)(O)O)C(=O)O`
ZINC1756826	1.000	255.1 Da LogP -1.79 TPSA 161.2	✓ Ro5	✓ Clean	`O=C(O)C[C@@H](NC(=O)CP(=O)(O)O)C(=O)O`
ZINC8215945	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)O[P@…`
ZINC13435042	0.959	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@](=O)(O)OP(=O…`
ZINC14960508	0.959	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](CO[P@](=O)(O)OP(=…`
ZINC142514175	0.818	483.2 Da LogP 0.19 TPSA 233.1	2 viol.	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
ZINC12503923	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c…`
ZINC12503924	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC1532581	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(…`
ZINC3645374	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC3861759	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=…`
ZINC3869816	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC3869817	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3869818	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC71404913	0.804	463.2 Da LogP 0.26 TPSA 209.7	1 viol.	✓ Clean	`C[P@@](=O)(O[P@@](=O)(O)OC[C@H]1O[C@@H](n2ccc(N…`
ZINC71404916	0.804	463.2 Da LogP 0.26 TPSA 209.7	1 viol.	✓ Clean	`C[P@@](=O)(O)O[P@@](C)(=O)O[P@@](=O)(O)OC[C@H]1…`
ZINC8215971	0.796	468.1 Da LogP -1.06 TPSA 244.4	2 viol.	✓ Clean	`O=c1nc(O)ccn1[C@H]1C[C@H](O)[C@@H](CO[P@@](=O)(…`
ZINC169292613	0.750	492.2 Da LogP 0.14 TPSA 278.7	1 viol.	Alert	`[N-]=[N+]=N[C@@H]1C[C@H](n2ccc(N)nc2=O)O[C@@H]1…`
ZINC111437949	0.741	481.2 Da LogP -0.72 TPSA 236.2	2 viol.	✓ Clean	`CNc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P…`
ZINC13516800	0.737	451.2 Da LogP -0.15 TPSA 230.0	1 viol.	✓ Clean	`Nc1ccn([C@H]2CC[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC32016993	0.737	451.2 Da LogP -0.15 TPSA 230.0	1 viol.	✓ Clean	`Nc1ccn([C@@H]2CC[C@H](CO[P@@](=O)(O)O[P@](=O)(O…`
ZINC12502055	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC12502057	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC12502058	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13431057	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13431059	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC25726736	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC3861746	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@@](=O)(O)…`
ZINC53683723	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC82142138	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC82142140	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC218114467	0.724	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC31440313	0.724	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC142487928	0.719	483.2 Da LogP -1.48 TPSA 270.4	2 viol.	✓ Clean	`Nc1nc(=O)n([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)…`
ZINC13588928	0.712	469.2 Da LogP -0.24 TPSA 230.0	1 viol.	✓ Clean	`Nc1ccn([C@@H]2CS[C@H](CO[P@](=O)(O)O[P@](=O)(O)…`
ZINC104864216	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@](=O)(O)OP(=O)(O)O)[C…`
ZINC12504412	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC12504413	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC12504414	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431045	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431047	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC13548733	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC33913782	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC8215624	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC58633440	0.695	482.2 Da LogP -2.25 TPSA 276.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC62612120	0.695	481.2 Da LogP -0.87 TPSA 250.2	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC81982895	0.695	482.2 Da LogP -2.25 TPSA 276.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC81982899	0.695	482.2 Da LogP -2.25 TPSA 276.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=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.