Protein profile

PA1267

hypothetical protein

Genome: NC_002516.2

Gene: PA1267 Structure source: AlphaFold UniProt Q9I477
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Amino acids 371
Annotations 3
Features 15
PDB binders 5
Druggability 0.709

Overview

Basic information about this protein and its source genome.

Accession
PA1267
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1267
Status
annotated
Amino acids
371
Structure source
AlphaFold
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. GO:0019470 The chemical reactions and pathways resulting in the breakdown of trans-4-hydroxy-L-proline.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
22.343
Human E-value
4.92e-10
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
CytoplasmicMembrane

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 0.709
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

3
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
  • GO:0019470 The chemical reactions and pathways resulting in the breakdown of trans-4-hydroxy-L-proline.

Sequence Features

Domain/signature hits from InterPro and related databases.

15 records
Show feature table
Start End DB Term Name
5 343 Pfam PF01266 FAD dependent oxidoreductase
5 343 InterPro IPR006076 FAD dependent oxidoreductase
5 13 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
4 363 SUPERFAMILY SSF51905 FAD/NAD(P)-binding domain
4 363 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
19 371 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1 18 Phobius SIGNAL_PEPTIDE Signal peptide region
14 18 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
204 304 SUPERFAMILY SSF54373 FAD-linked reductases, C-terminal domain
1 4 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
3 367 PANTHER PTHR13847 SARCOSINE DEHYDROGENASE-RELATED
81 304 Gene3D G3DSA:3.30.9.10 -
5 343 Gene3D G3DSA:3.50.50.60 -
5 343 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
87 107 Coils Coil Coil

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 PA1267
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 0.709
2 0.237

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
16A
5HXW
Q9LCB2 284.6 Da LogP 6.17 TPSA 0.0 1 viol. ✓ Clean CCCCCCCCCCCCCCCC[N+](C)(C)C
AAC
1NG3
O31616 117.1 Da LogP -0.79 TPSA 66.4 ✓ Ro5 ✓ Clean CC(=O)NCC(=O)O
B6X
6J39
X5IYZ1 248.3 Da LogP 2.62 TPSA 74.6 ✓ Ro5 ✓ Clean CCCCCC[C@H](CC(=O)O)SCC(=O)O
GOA
1RYI
O31616 76.1 Da LogP -0.94 TPSA 57.5 ✓ Ro5 ✓ Clean C(C(=O)O)O
PEO
1NG4
O31616 34.0 Da LogP 0.02 TPSA 40.5 ✓ Ro5 ✓ Clean OO

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.