Protein profile

PA4215

trans-2,3-dihydro-3-hydroxyanthranilate isomerase

Genome: NC_002516.2

Gene: PA4215 phzF1 phzF2 PA1904; phzF Structure source: AlphaFold UniProt O69754
Export view
Amino acids 278
Annotations 7
Features 11
PDB binders 5
Druggability 0.669

Overview

Basic information about this protein and its source genome.

Accession
PA4215
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA4215 phzF1 phzF2 PA1904; phzF
Status
annotated
Amino acids
278
Structure source
AlphaFold
EC
5.3.3.17
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0016853 Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5. GO:0102943 Catalysis of the reaction: (2S,3S)-2,3-dihydro-3-hydroxyanthranilic acid = (1R,6S)-6-ammonio-5-oxocyclohex-2-ene-1-carboxylate. GO:0002047 The chemical reactions and pathways resulting in the formation of a phenazine antibiotic, a polycyclic pyrazine with two nitrogen atoms in the ring. 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. GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
27.984
Human E-value
2.08e-10
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 0.669
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MHRYVVIDAFASEPLQGNPVAVFFDCDDLSGERMQRMAREMNLSESTFVLRPQQDGDARIRIFTPVNELPFAGHPLLGTAIALGAETDKDRLFLETRMGTVPFALERQDGKVVACSMQQPIPTWEHFSRPAELLAALGLKGSTFPIEVYRNGPRHVFVGLESVAALSALHPDHRALCDFPDLAVNCFAGAGRHWRSRMFSPAYGVVEDAATGSAAGPLAIHLARHRQIPYGQQIEILQGVEIGRPSRMYARAEGAGERVSAVEVSGNGAAFAEGRAYL

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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0016853 Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
  • GO:0102943 Catalysis of the reaction: (2S,3S)-2,3-dihydro-3-hydroxyanthranilic acid = (1R,6S)-6-ammonio-5-oxocyclohex-2-ene-1-carboxylate.
  • GO:0002047 The chemical reactions and pathways resulting in the formation of a phenazine antibiotic, a polycyclic pyrazine with two nitrogen atoms in the ring.
  • 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.
  • GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.

Sequence Features

Domain/signature hits from InterPro and related databases.

11 records
Show feature table
Start End DB Term Name
1 278 PIRSF PIRSF016184 Ismrse_PhzF
1 278 InterPro IPR003719 Phenazine biosynthesis PhzF-like
120 266 Gene3D G3DSA:3.10.310.10 Diaminopimelate Epimerase; Chain A, domain 1
3 275 PANTHER PTHR13774 PHENAZINE BIOSYNTHESIS PROTEIN
3 275 InterPro IPR003719 Phenazine biosynthesis PhzF-like
7 119 Gene3D G3DSA:3.10.310.10 Diaminopimelate Epimerase; Chain A, domain 1
5 273 NCBIfam TIGR00654 PhzF family phenazine biosynthesis isomerase
5 273 InterPro IPR003719 Phenazine biosynthesis PhzF-like
2 277 SUPERFAMILY SSF54506 Diaminopimelate epimerase-like
7 274 Pfam PF02567 Phenazine biosynthesis-like protein
7 274 InterPro IPR003719 Phenazine biosynthesis PhzF-like

3D Structure

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

3D visualization script Full viewer

Loading 3D structure...

Legend High Medium Low

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 PA4215
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 0.669
2 0.368

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.

55 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
3HA
1U1W
Q51792 153.1 Da LogP 0.67 TPSA 83.5 ✓ Ro5 ✓ Clean c1cc(c(c(c1)O)N)C(=O)O
BTB
4DUN
Q186X0 209.2 Da LogP -3.01 TPSA 104.4 ✓ Ro5 ✓ Clean C(CO)N(CCO)C(CO)(CO)CO
HHA
1U1X
Q51792 155.2 Da LogP -0.74 TPSA 83.5 ✓ Ro5 ✓ Clean C1=C[C@@H]([C@H](C(=C1)C(=O)O)N)O
SIN
3EDN
A0A6L8PH16 118.1 Da LogP -0.06 TPSA 74.6 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)O
W81
5IWE
Q51792 183.2 Da LogP -1.75 TPSA 77.0 ✓ Ro5 ✓ Clean CCO[C@@H]1C=CC=C([C@H]1[NH3+])C(=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.