Protein profile

PA5172

ornithine carbamoyltransferase

Genome: NC_002516.2

Gene: PA5172 arcB Structure source: Experimental + AlphaFold UniProt P08308

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Amino acids 336

Annotations 10

Features 36

PDB binders 5

Druggability 0.596

Overview

Basic information about this protein and its source genome.

Accession: PA5172
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA5172 arcB
Status: annotated
Amino acids: 336
Structure source: Experimental + AlphaFold

2.1.3.3

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0016597 Binding to an amino acid, organic acids containing one or more amino substituents. GO:0004585 Catalysis of the reaction: carbamoyl phosphate + L-ornithine = phosphate + L-citrulline. GO:0019240 The chemical reactions and pathways resulting in the formation of citrulline, N5-carbamoyl-L-ornithine, an alpha amino acid not found in proteins. GO:0042450 OBSOLETE. The chemical reactions and pathways resulting in the formation of arginine (2-amino-5-guanidinopentanoic acid) via the intermediate compound ornithine. GO:0019546 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-arginine into other compounds, including ornithine and CO2, using the enzyme arginine deiminase.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 38.889
Human E-value: 3.54e-06
Gut microbiome off-target: hit
Essential (DEG): N
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 0.596

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MAFNMHNRNLLSLMHHSTRELRYLLDLSRDLKRAKYTGTEQQHLKRKNIALIFEKTSTRTRCAFEVAAYDQGANVTYIDPNSSQIGHKESMKDTARVLGRMYDAIEYRGFKQEIVEELAKFAGVPVFNGLTDEYHPTQMLADVLTMREHSDKPLHDISYAYLGDARNNMGNSLLLIGAKLGMDVRIAAPKALWPHDEFVAQCKKFAEESGAKLTLTEDPKEAVKGVDFVHTDVWVSMGEPVEAWGERIKELLPYQVNMEIMKATGNPRAKFMHCLPAFHNSETKVGKQIAEQYPNLANGIEVTEDVFESPYNIAFEQAENRMHTIKAILVSTLADI

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

2.1.3.3

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0016597 Binding to an amino acid, organic acids containing one or more amino substituents.
GO:0004585 Catalysis of the reaction: carbamoyl phosphate + L-ornithine = phosphate + L-citrulline.
GO:0019240 The chemical reactions and pathways resulting in the formation of citrulline, N5-carbamoyl-L-ornithine, an alpha amino acid not found in proteins.
GO:0042450 OBSOLETE. The chemical reactions and pathways resulting in the formation of arginine (2-amino-5-guanidinopentanoic acid) via the intermediate compound ornithine.
GO:0019546 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-arginine into other compounds, including ornithine and CO2, using the enzyme arginine deiminase.
GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
GO:0016743 Catalysis of the transfer of a carboxyl- or carbamoyl group from one compound (donor) to another (acceptor).
GO:0006591 The chemical reactions and pathways involving ornithine, an amino acid only rarely found in proteins, but which is important in living organisms as an intermediate in the reactions of the urea cycle and in arginine biosynthesis.

Sequence Features

Domain/signature hits from InterPro and related databases.

36 records

Show feature table

Start	End	DB	Term	Name
7	334	Hamap	MF_01109	Ornithine carbamoyltransferase, catabolic [argI].
7	334	InterPro	IPR024904	Ornithine carbamoyltransferase
8	333	NCBIfam	TIGR00658	ornithine carbamoyltransferase
8	333	InterPro	IPR002292	Ornithine/putrescine carbamoyltransferase
135	146	PRINTS	PR00100	Aspartate/ornithine carbamoyltransferase superfamily signature
135	146	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
53	72	PRINTS	PR00100	Aspartate/ornithine carbamoyltransferase superfamily signature
53	72	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
267	276	PRINTS	PR00100	Aspartate/ornithine carbamoyltransferase superfamily signature
267	276	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
298	321	PRINTS	PR00100	Aspartate/ornithine carbamoyltransferase superfamily signature
298	321	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
5	333	Gene3D	G3DSA:3.40.50.1370	Aspartate/ornithine carbamoyltransferase
5	333	InterPro	IPR036901	Aspartate/ornithine carbamoyltransferase superfamily
152	320	Gene3D	G3DSA:3.40.50.1370	Aspartate/ornithine carbamoyltransferase
152	320	InterPro	IPR036901	Aspartate/ornithine carbamoyltransferase superfamily
3	333	PANTHER	PTHR45753	ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL
8	148	Pfam	PF02729	Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain
8	148	InterPro	IPR006132	Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding
5	162	FunFam	G3DSA:3.40.50.1370:FF:000003	Ornithine carbamoyltransferase
156	331	Pfam	PF00185	Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain
156	331	InterPro	IPR006131	Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain
4	334	SUPERFAMILY	SSF53671	Aspartate/ornithine carbamoyltransferase
4	334	InterPro	IPR036901	Aspartate/ornithine carbamoyltransferase superfamily
53	60	ProSitePatterns	PS00097	Aspartate and ornithine carbamoyltransferases signature.
53	60	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
84	97	PRINTS	PR00102	Ornithine carbamoyltransferase signature
84	97	InterPro	IPR002292	Ornithine/putrescine carbamoyltransferase
229	239	PRINTS	PR00102	Ornithine carbamoyltransferase signature
229	239	InterPro	IPR002292	Ornithine/putrescine carbamoyltransferase
51	65	PRINTS	PR00102	Ornithine carbamoyltransferase signature
51	65	InterPro	IPR002292	Ornithine/putrescine carbamoyltransferase
124	138	PRINTS	PR00102	Ornithine carbamoyltransferase signature
124	138	InterPro	IPR002292	Ornithine/putrescine carbamoyltransferase
312	323	PRINTS	PR00102	Ornithine carbamoyltransferase signature
312	323	InterPro	IPR002292	Ornithine/putrescine carbamoyltransferase

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

2 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
PDB 1DXH	X-ray	2.50 Å	A	99.7% 2-336	PDBe RCSB PDBj File	Viewing
PDB 1ORT	X-ray	3.00 Å	A,B,C,D,E,F,G,H,I,J,K,L	99.7% 2-336	PDBe RCSB PDBj File	Loaded
AlphaFold PA5172	AlphaFold	—	—	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				0.596

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	7.3	0.381
2	2.94	0.094
3	0.73	0.002

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				0.49
3				0.313

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.

56 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
CIR	4JQO	Q8DCF5	175.2 Da LogP -1.15 TPSA 118.4	✓ Ro5	✓ Clean	`C(C[C@@H](C(=O)O)N)CNC(=O)N`
CP	1C9Y	P00480	141.0 Da LogP -0.83 TPSA 109.9	✓ Ro5	✓ Clean	`C(=O)(N)OP(=O)(O)O`
NVA	1C9Y	P00480	117.1 Da LogP 0.20 TPSA 63.3	✓ Ro5	✓ Clean	`CCC[C@@H](C(=O)O)N`
PE5	4H31	Q8DCF5	398.5 Da LogP 0.13 TPSA 94.1	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCOCCO`
PSQ	1DUV	P04391	290.2 Da LogP -1.77 TPSA 184.8	1 viol.	✓ Clean	`C(C[C@@H](C(=O)O)N)CN[P@](=O)(N)NS(=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
PAO	P00480	7.00	254.2 Da LogP -1.53 TPSA 149.9	✓ Ro5	✓ Clean	`C(C[C@@H](C(=O)O)N)CNC(=O)CP(=O)(O)O`

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
ZINC5650743	1.000	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917	1.000	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC12501520	0.688	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC3874716	0.688	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769	0.688	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548	0.688	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829	0.688	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830	0.688	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5859031	0.688	294.4 Da LogP 1.13 TPSA 55.4	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCC`
ZINC1570993	0.667	215.3 Da LogP 2.93 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@H](N)C(=O)O`
ZINC1570999	0.667	229.4 Da LogP 3.32 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCCC[C@H](N)C(=O)O`
ZINC1620974	0.667	243.4 Da LogP 3.71 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[C@H](N)C(=O)O`
ZINC1742220	0.667	201.3 Da LogP 2.54 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCC[C@H](N)C(=O)O`
ZINC2035155	0.667	215.3 Da LogP 2.93 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@@H](N)C(=O)O`
ZINC2035157	0.667	201.3 Da LogP 2.54 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCC[C@@H](N)C(=O)O`
ZINC2037129	0.667	243.4 Da LogP 3.71 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[C@@H](N)C(=O)O`
ZINC43531622	0.667	271.4 Da LogP 4.49 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC[C@H](N)C(=O)O`
ZINC43531626	0.667	271.4 Da LogP 4.49 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC[C@@H](N)C(=O)O`
ZINC8437446	0.667	229.4 Da LogP 3.32 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCCC[C@@H](N)C(=O)O`
ZINC196899382	0.625	228.2 Da LogP -0.14 TPSA 92.4	✓ Ro5	✓ Clean	`N[C@@H](CCCNC(=O)C(F)(F)F)C(=O)O`
ZINC65356716	0.625	205.3 Da LogP -0.35 TPSA 98.2	✓ Ro5	✓ Clean	`CSC(=O)[C@@H](N)CCCNC(N)=O`
ZINC1644613	0.619	206.3 Da LogP 0.83 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCO`
ZINC3055005	0.619	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	0.619	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	0.619	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC27644247	0.618	230.3 Da LogP 0.09 TPSA 111.2	✓ Ro5	✓ Clean	`CCCCNC(=N)NCCC[C@H](N)C(=O)O`
ZINC4155291	0.618	216.2 Da LogP -1.37 TPSA 130.8	✓ Ro5	✓ Clean	`CC(=O)/N=C(\N)NCCC[C@H](N)C(=O)O`
ZINC4155299	0.618	216.2 Da LogP -1.37 TPSA 130.8	✓ Ro5	✓ Clean	`CC(=O)/N=C(\N)NCCC[C@@H](N)C(=O)O`
ZINC1529718	0.606	202.3 Da LogP -0.74 TPSA 102.4	✓ Ro5	✓ Clean	`CN(C)C(=N)NCCC[C@H](N)C(=O)O`
ZINC1546170	0.606	216.3 Da LogP -0.30 TPSA 111.2	✓ Ro5	✓ Clean	`CCCNC(=N)NCCC[C@H](N)C(=O)O`
ZINC2560273	0.606	202.3 Da LogP -0.69 TPSA 111.2	✓ Ro5	✓ Clean	`CCNC(=N)NCCC[C@H](N)C(=O)O`
ZINC4543782	0.606	202.3 Da LogP -0.74 TPSA 102.4	✓ Ro5	✓ Clean	`CN(C)C(=N)NCCC[C@@H](N)C(=O)O`
ZINC7997269	0.606	205.3 Da LogP 0.07 TPSA 99.2	✓ Ro5	✓ Clean	`CSC(=N)NCCC[C@@H](N)C(=O)O`
ZINC1580161	0.600	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118	0.600	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257	0.600	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654	0.600	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44076059	0.600	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101	0.600	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5997860	0.600	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC144076260	0.594	232.2 Da LogP -0.84 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CC(=O)O)C(=O)O`
ZINC218922593	0.594	204.2 Da LogP -1.32 TPSA 112.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CO)C(=O)O`
ZINC2516116	0.594	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC4545887	0.594	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC4545888	0.594	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)NCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC4545889	0.594	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@H](CCCCNC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC50027904	0.594	261.3 Da LogP -1.51 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)C[C@H](N)C(=O)O)C(=O)O`
ZINC1555367	0.591	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720128	0.591	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC2555269	0.591	220.3 Da LogP 1.22 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCOCCOCCOCCO`

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.