Protein profile

PA0310

hypothetical protein

Genome: NC_002516.2

Gene: PA0310 Structure source: AlphaFold UniProt Q9I6I1
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Amino acids 232
Annotations 6
Features 8
PDB binders 2
Druggability 0.673

Overview

Basic information about this protein and its source genome.

Accession
PA0310
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA0310
Status
annotated
Amino acids
232
Structure source
AlphaFold
GO
GO:0008198 Binding to a ferrous iron ion, Fe(II). GO:0031418 Binding to L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species. GO:0031543 Catalysis of the reaction: peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl hydroxy-L-proline + succinate + CO2. GO:0071456 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. GO:0016705 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from each of two donors, and molecular oxygen is reduced or incorporated into a donor. GO:0005506 Binding to an iron (Fe) ion.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
34.375
Human E-value
1.71e-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 0.673
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MGRYCRHAADRLSRHRGGTLQWTMHINVNHPLLHRIVDELVDQGWSHQSIFMPERLTTRLAEECRTRAVAGDLTPAAIGRGDGQVIREGIRGDLTQWLEPGESEACDEYLGVMDSLRQALNASLFLGLEDFECHFALYPPGAYYQKHVDRFRDDDARTVSAVLYLNDAWLPEHGGALRLHLPQRQVDIQPTGGSLVVFMSAGTEHEVLPASRDRLSLTGWFRRRNESLLQLS

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6
  • GO:0008198 Binding to a ferrous iron ion, Fe(II).
  • GO:0031418 Binding to L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.
  • GO:0031543 Catalysis of the reaction: peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl hydroxy-L-proline + succinate + CO2.
  • GO:0071456 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
  • GO:0016705 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from each of two donors, and molecular oxygen is reduced or incorporated into a donor.
  • GO:0005506 Binding to an iron (Fe) ion.

Sequence Features

Domain/signature hits from InterPro and related databases.

8 records
Show feature table
Start End DB Term Name
129 223 ProSiteProfiles PS51471 Fe(2+) 2-oxoglutarate dioxygenase domain profile.
129 223 InterPro IPR005123 Oxoglutarate/iron-dependent dioxygenase
27 226 PANTHER PTHR12907 EGL NINE HOMOLOG-RELATED
134 222 Pfam PF13640 2OG-Fe(II) oxygenase superfamily
134 222 InterPro IPR044862 Prolyl 4-hydroxylase alpha subunit, Fe(2+) 2OG dioxygenase domain
31 228 Gene3D G3DSA:2.60.120.620 q2cbj1_9rhob like domain
43 222 SMART SM00702 p4hc
43 222 InterPro IPR006620 Prolyl 4-hydroxylase, alpha subunit

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

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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 PA0310
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
2 0.673
1 0.251

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.

152 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
5C5T
Q84406 146.1 Da LogP -0.50 TPSA 91.7 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)C(=O)O
OGA
6F0W
I6QVT6 147.1 Da LogP -1.73 TPSA 103.7 ✓ Ro5 ✓ Clean C(C(=O)O)NC(=O)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.