Protein profile

PA5025

O-acetylhomoserine aminocarboxypropyltransferase

Genome: NC_002516.2

Gene: PA5025 metY Structure source: AlphaFold UniProt Q9HUE4
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Amino acids 425
Annotations 7
Features 19
PDB binders 19
Druggability 0.653

Overview

Basic information about this protein and its source genome.

Accession
PA5025
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA5025 metY
Status
annotated
Amino acids
425
Structure source
AlphaFold
GO
GO:0004124 Catalysis of the reaction: O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate. GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. GO:0071269 The chemical reactions and pathways resulting in the formation of L-homocysteine. GO:0019346 The interconversion of homocysteine and cysteine via cystathionine. In contrast with enteric bacteria and mammals, Saccharomyces cerevisiae has two transsulfuration pathways employing two separate sets of enzymes. GO:0016765 Catalysis of the transfer of an alkyl or aryl (but not methyl) group from one compound (donor) to another (acceptor). GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
35.915
Human E-value
1.34e-62
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 0.653
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

7
  • GO:0004124 Catalysis of the reaction: O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate.
  • GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
  • GO:0071269 The chemical reactions and pathways resulting in the formation of L-homocysteine.
  • GO:0019346 The interconversion of homocysteine and cysteine via cystathionine. In contrast with enteric bacteria and mammals, Saccharomyces cerevisiae has two transsulfuration pathways employing two separate sets of enzymes.
  • GO:0016765 Catalysis of the transfer of an alkyl or aryl (but not methyl) group from one compound (donor) to another (acceptor).
  • GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Sequence Features

Domain/signature hits from InterPro and related databases.

19 records
Show feature table
Start End DB Term Name
1 285 FunFam G3DSA:3.40.640.10:FF:000035 O-succinylhomoserine sulfhydrylase
2 421 NCBIfam TIGR01326 O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
2 421 InterPro IPR006235 O-acetylhomoserine/O-acetylserine sulfhydrylase
196 210 ProSitePatterns PS00868 Cys/Met metabolism enzymes pyridoxal-phosphate attachment site.
196 210 InterPro IPR000277 Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
4 420 Pfam PF01053 Cys/Met metabolism PLP-dependent enzyme
4 420 InterPro IPR000277 Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
289 425 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
289 425 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain
1 424 PIRSF PIRSF001434 CGS
1 424 InterPro IPR000277 Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
1 285 Gene3D G3DSA:3.40.640.10 -
1 285 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major domain
1 421 SUPERFAMILY SSF53383 PLP-dependent transferases
1 421 InterPro IPR015424 Pyridoxal phosphate-dependent transferase
2 422 PANTHER PTHR43797 HOMOCYSTEINE/CYSTEINE SYNTHASE
2 422 InterPro IPR006235 O-acetylhomoserine/O-acetylserine sulfhydrylase
20 412 CDD cd00614 CGS_like
20 412 InterPro IPR000277 Cys/Met metabolism, pyridoxal phosphate-dependent enzyme

3D Structure

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

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Structural evidence

0 + 1

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA5025
AlphaFold — — full sequence — Viewing
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 0.645
5 0.437

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.

69 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
0JO
4IYO
Q5H4T8 316.2 Da LogP 0.72 TPSA 149.5 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/C(=C)C(=O)O)O
2LM
3AEL
Q86D28 378.3 Da LogP 1.48 TPSA 149.5 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)C/N=C(\CCSC)/C(=O)O)O
3LM
3AEO
Q86D28 378.3 Da LogP 1.13 TPSA 149.2 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN/C(=C/CSC)/C(=O)O)O
4LM
3AEP
Q86D28 330.2 Da LogP 1.11 TPSA 149.5 ✓ Ro5 ✓ Clean C/C=C(\C(=O)O)/N=C/c1c(cnc(c1O)C)COP(=O)(O)O
7XF
5X30
P13254 366.3 Da LogP 0.57 TPSA 149.2 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CCS)C(=O)O)O
AA5
3AEJ
Q86D28 378.3 Da LogP 1.33 TPSA 149.5 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)C=N[C@@H](CCSC)C(=O)O)O
ECX
3JW9
Q84AR1 149.2 Da LogP 0.15 TPSA 63.3 ✓ Ro5 ✓ Clean CCSC[C@@H](C(=O)O)N
H2S
5X2X
P13254 34.1 Da LogP 0.11 TPSA 0.0 ✓ Ro5 ✓ Clean S
HCS
3VK4
P13254 135.2 Da LogP -0.28 TPSA 63.3 ✓ Ro5 ✓ Clean C(CS)[C@@H](C(=O)O)N
KOU
4IY7
Q5H4T8 334.2 Da LogP -0.43 TPSA 169.8 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/C(CO)C(=O)O)O
LCS
4OMA
Q84AR1 331.2 Da LogP -0.29 TPSA 150.6 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)C/N=C/2\CONC2=O)O
MEE
3AEP
Q86D28 48.1 Da LogP 0.55 TPSA 0.0 ✓ Ro5 ✓ Clean CS
MPJ
3JWA
Q84AR1 169.2 Da LogP 0.49 TPSA 63.3 ✓ Ro5 ✓ Clean CSCC[C@H](N)[P@H](=O)O
NAK
4IYO
Q5H4T8 87.1 Da LogP -3.04 TPSA 65.7 ✓ Ro5 ✓ Clean CC(=[NH2+])C(=O)[O-]
NLE
5M3Z
A0A0A5P8W7 131.2 Da LogP 0.59 TPSA 63.3 ✓ Ro5 ✓ Clean CCCC[C@@H](C(=O)O)N
PLG
4HF8
Q84AR1 306.2 Da LogP -0.12 TPSA 149.2 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CNCC(=O)O)O
PY6
5M3Z
A0A0A5P8W7 362.3 Da LogP 1.44 TPSA 149.2 ✓ Ro5 ✓ Clean CCCC[C@@H](C(=O)O)NCc1c(cnc(c1O)C)COP(=O)(O)O
PYR
4IYO
Q5H4T8 88.1 Da LogP -0.34 TPSA 54.4 ✓ Ro5 ✓ Clean CC(=O)C(=O)O
PZP
3MKJ
Q84AR1 246.2 Da LogP 0.70 TPSA 123.7 ✓ Ro5 ✓ Clean [H]/N=C/c1c(cnc(c1O)C)COP(=O)(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.