Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA5214
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: gcvH1
Status: annotated
Amino acids: 129
Structure source: ColabFold

GO

GO:0005960 A protein complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase, also known as L, P, H, and T. GO:0019464 The chemical reactions and pathways resulting in the breakdown of glycine by oxidative cleavage to carbon dioxide, ammonia, and a methylene group, mediated by enzymes of the glycine cleavage complex.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 55.056
Human E-value: 2.21e-26
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Unknown

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 GO

Gene Ontology (GO)

2

GO:0005960 A protein complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase, also known as L, P, H, and T.
GO:0019464 The chemical reactions and pathways resulting in the breakdown of glycine by oxidative cleavage to carbon dioxide, ammonia, and a methylene group, mediated by enzymes of the glycine cleavage complex.

Sequence Features

Domain/signature hits from InterPro and related databases.

16 records

Show feature table

Start	End	DB	Term	Name
5	126	Hamap	MF_00272	Glycine cleavage system H protein [gcvH].
5	126	InterPro	IPR002930	Glycine cleavage system H-protein
1	126	Gene3D	G3DSA:2.40.50.100	-
8	125	Pfam	PF01597	Glycine cleavage H-protein
8	125	InterPro	IPR033753	Glycine cleavage system H-protein/Simiate
24	105	ProSiteProfiles	PS50968	Biotinyl/lipoyl domain profile.
24	105	InterPro	IPR000089	Biotin/lipoyl attachment
5	126	PANTHER	PTHR11715	GLYCINE CLEAVAGE SYSTEM H PROTEIN
10	104	CDD	cd06848	GCS_H
10	104	InterPro	IPR033753	Glycine cleavage system H-protein/Simiate
49	78	ProSitePatterns	PS00189	2-oxo acid dehydrogenases acyltransferase component lipoyl binding site.
49	78	InterPro	IPR003016	2-oxo acid dehydrogenase, lipoyl-binding site
3	126	SUPERFAMILY	SSF51230	Single hybrid motif
3	126	InterPro	IPR011053	Single hybrid motif
3	127	NCBIfam	TIGR00527	glycine cleavage system protein GcvH
3	127	InterPro	IPR017453	Glycine cleavage system H-protein, subgroup

3D Structure

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

No pockets are loaded yet for the displayed ColabFold model PA5214 structure. Run experimental pocket backfill to show FPocket/P2Rank overlays on this structure.

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Structural evidence

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
ColabFold PA5214	ColabFold	—	—	full sequence	—	Viewing

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.

17 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
LPB	1HPC	P16048	206.3 Da LogP 2.79 TPSA 37.3	✓ Ro5	✓ Clean	`C1CSS[C@H]1CCCCC(=O)O`
OSS	1HTP	P16048	313.5 Da LogP 2.41 TPSA 83.5	✓ Ro5	✓ Clean	`C(CCC(=O)O)C[C@@H](CCSCN)SSCCO`
RED	1DXM	P16048	208.3 Da LogP 2.25 TPSA 37.3	✓ Ro5	✓ Clean	`C(CCC(=O)O)C[C@H](CCS)S`

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
ZINC1529363	1.000	208.3 Da LogP 2.25 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCC[C@H](S)CCS`
ZINC3869601	1.000	208.3 Da LogP 2.25 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCC[C@@H](S)CCS`
ZINC12954423	0.538	232.4 Da LogP 3.90 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCS`
ZINC2164257	0.538	218.4 Da LogP 3.51 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCS`
ZINC90745150	0.538	260.4 Da LogP 4.68 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCS`
ZINC2151107	0.500	231.3 Da LogP 1.60 TPSA 100.6	✓ Ro5	✓ Clean	`NC(CCCCC(=O)O)CCCCC(=O)O`
ZINC2839271	0.500	245.3 Da LogP 1.99 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC(=O)O)CCCCC(=O)O`
ZINC2839272	0.500	245.3 Da LogP 1.99 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCC(=O)O)CCCCC(=O)O`
ZINC44713478	0.500	260.4 Da LogP 3.06 TPSA 77.8	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(O)O`
ZINC4783630	0.500	346.5 Da LogP 3.34 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC[C@H](O)[C@H](O)CCCCCCCC(=O)O`
ZINC4783631	0.500	346.5 Da LogP 3.34 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC[C@@H](O)[C@H](O)CCCCCCCC(=O)O`
ZINC4783632	0.500	346.5 Da LogP 3.34 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC[C@H](O)[C@@H](O)CCCCCCCC(=O)O`
ZINC4956318	0.500	273.4 Da LogP 2.77 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCCCC(=O)O)CCCCC(=O)O`
ZINC4956319	0.500	273.4 Da LogP 2.77 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCCCC(=O)O)CCCCC(=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.