Protein profile

PA2964

4-amino-4-deoxychorismate lyase

Genome: NC_002516.2

Gene: PA2964 pabC Structure source: Experimental + AlphaFold UniProt Q9HZN6
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Amino acids 271
Annotations 7
Features 14
PDB binders 8
Druggability 0.486

Overview

Basic information about this protein and its source genome.

Accession
PA2964
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA2964 pabC
Status
annotated
Amino acids
271
Structure source
Experimental + AlphaFold
EC
4.1.3.38
GO
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0008696 Catalysis of the reaction: 4-amino-4-deoxychorismate = 4-aminobenzoate + H+ + pyruvate. 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:0008153 The chemical reactions and pathways resulting in the formation of 4-aminobenzoate, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins. GO:0046656 The chemical reactions and pathways resulting in the formation of folic acid, pteroylglutamic acid. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
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 0.486
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0008696 Catalysis of the reaction: 4-amino-4-deoxychorismate = 4-aminobenzoate + H+ + pyruvate.
  • 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:0008153 The chemical reactions and pathways resulting in the formation of 4-aminobenzoate, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins.
  • GO:0046656 The chemical reactions and pathways resulting in the formation of folic acid, pteroylglutamic acid.
  • 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.

14 records
Show feature table
Start End DB Term Name
17 265 CDD cd01559 ADCL_like
17 265 InterPro IPR017824 Aminodeoxychorismate lyase, class IV
112 270 FunFam G3DSA:3.20.10.10:FF:000002 D-alanine aminotransferase
4 263 SUPERFAMILY SSF56752 D-aminoacid aminotransferase-like PLP-dependent enzymes
4 263 InterPro IPR036038 Aminotransferase-like, PLP-dependent enzymes
112 271 Gene3D G3DSA:3.20.10.10 -
112 271 InterPro IPR043132 Branched-chain-amino-acid aminotransferase-like, C-terminal
4 263 NCBIfam TIGR03461 aminodeoxychorismate lyase
4 263 InterPro IPR017824 Aminodeoxychorismate lyase, class IV
2 111 Gene3D G3DSA:3.30.470.10 -
2 111 InterPro IPR043131 Branched-chain-amino-acid aminotransferase-like, N-terminal
25 246 Pfam PF01063 Amino-transferase class IV
25 246 InterPro IPR001544 Aminotransferase class IV
2 268 PANTHER PTHR42743 AMINO-ACID AMINOTRANSFERASE

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

1 + 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 2Y4R
X-ray 1.75 Å A,B
100.0% 1-271
PDBe RCSB PDBj File
Viewing
AlphaFold PA2964
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
3 0.486
2 0.333

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 14.42 0.722
2 7.98 0.424
3 3.12 0.105
4 2.05 0.045

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.

71 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
AKG
5E25
A0A0A7GJ30 146.1 Da LogP -0.50 TPSA 91.7 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)C(=O)O
DCS
2DAA
P19938 333.2 Da LogP -0.78 TPSA 150.2 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H]2CONC2=O)O
PDD
3DAA
P19938 320.2 Da LogP 0.27 TPSA 149.2 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@H](C)C(=O)O)O
PDG
4CE5
Q0C8G1 378.3 Da LogP 0.11 TPSA 186.5 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@H](CCC(=O)O)C(=O)…
PMP
1A0G
P19938 248.2 Da LogP 0.16 TPSA 125.9 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN)O
PSZ
3LQS
P19938 374.3 Da LogP 2.08 TPSA 149.2 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CNc2cc(sc2)C(=O)O)O
PXG
5MR0
O29329 368.3 Da LogP 2.02 TPSA 149.2 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CNc2cccc(c2)C(=O)O)O
TAM
5MQZ
O29329 163.2 Da LogP -1.17 TPSA 86.7 ✓ Ro5 ✓ Clean C(CO)C(CCO)(CCO)N

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.