Protein profile

PA0305

hypothetical protein

Genome: NC_002516.2

Gene: PA0305 Structure source: AlphaFold UniProt Q9I6I6
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Amino acids 795
Annotations 5
Features 23
PDB binders 27
Druggability 0.906

Overview

Basic information about this protein and its source genome.

Accession
PA0305
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA0305
Status
annotated
Amino acids
795
Structure source
AlphaFold
GO
GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria). GO:0016811 Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amide. GO:0046872 Binding to a metal ion. GO:0017000 The chemical reactions and pathways resulting in the formation of an antibiotic, a substance produced by or derived from certain fungi, bacteria, and other organisms, that can destroy or inhibit the growth of other microorganisms. GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Periplasmic

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 0.906
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5
  • GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
  • GO:0016811 Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amide.
  • GO:0046872 Binding to a metal ion.
  • GO:0017000 The chemical reactions and pathways resulting in the formation of an antibiotic, a substance produced by or derived from certain fungi, bacteria, and other organisms, that can destroy or inhibit the growth of other microorganisms.
  • GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.

Sequence Features

Domain/signature hits from InterPro and related databases.

23 records
Show feature table
Start End DB Term Name
1 794 PIRSF PIRSF001227 Pen_acylase
1 794 InterPro IPR014395 Penicillin/GL-7-ACA/AHL acylase
248 773 Gene3D G3DSA:3.60.20.10 Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
248 773 InterPro IPR029055 Nucleophile aminohydrolases, N-terminal
5 16 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
5 24 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
248 538 CDD cd03747 Ntn_PGA_like
17 25 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
13 176 Gene3D G3DSA:1.10.439.10 Penicillin Amidohydrolase, domain 1
13 176 InterPro IPR023343 Penicillin amidase type, domain 1
42 782 Pfam PF01804 Penicillin amidase
42 782 InterPro IPR002692 Penicillin/GL-7-ACA/AHL/aculeacin-A acylase
1 4 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
542 678 Gene3D G3DSA:1.10.1400.10 -
542 678 InterPro IPR043147 Penicillin amidase type, A-knob
39 794 SUPERFAMILY SSF56235 N-terminal nucleophile aminohydrolases (Ntn hydrolases)
39 794 InterPro IPR029055 Nucleophile aminohydrolases, N-terminal
2 793 PANTHER PTHR34218 PEPTIDASE S45 PENICILLIN AMIDASE
2 793 InterPro IPR002692 Penicillin/GL-7-ACA/AHL/aculeacin-A acylase
320 391 Gene3D G3DSA:2.30.120.10 -
320 391 InterPro IPR043146 Penicillin amidase type, N-terminal domain, B-knob
1 25 Phobius SIGNAL_PEPTIDE Signal peptide region
26 795 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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 PA0305
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
3 0.906
24 0.208

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.

94 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
28N
3SRC
Q9I194 269.1 Da LogP 1.48 TPSA 57.3 ✓ Ro5 ✓ Clean c1cc2c(cc1Br)N3C(=NOC3=O)CO2
28S
3SRB
Q9I194 264.1 Da LogP 2.99 TPSA 37.8 ✓ Ro5 ✓ Clean C=CCNc1c2cc(ccc2ncn1)Br
3LA
2WYC
Q9I194 214.3 Da LogP 3.17 TPSA 54.4 ✓ Ro5 ✓ Clean CCCCCCCCCC(=O)CC(=O)O
3QD
4WKS
Q9I194 73.9 Da LogP -0.52 TPSA 40.5 ✓ Ro5 ✓ Clean B(CC)(O)O
3QJ
4WKU
Q9I194 147.0 Da LogP 0.48 TPSA 60.7 ✓ Ro5 ✓ Clean [B-](CCCCCC)(O)(O)O
3QK
4WKV
Q9I194 175.1 Da LogP 1.26 TPSA 60.7 ✓ Ro5 ✓ Clean [B-](CCCCCCCC)(O)(O)O
4HP
1AI6
P06875 152.1 Da LogP 1.02 TPSA 57.5 ✓ Ro5 ✓ Clean c1cc(ccc1CC(=O)O)O
83M
5UBK
Q9I194 658.8 Da LogP 2.83 TPSA 212.3 2 viol. ✓ Clean CCCCCCCCCCCCCC(=O)N[C@@H](CCC(=O)N[C@H](Cc1ccc(…
A08
4K2F
Q9I194 263.1 Da LogP 4.04 TPSA 36.7 ✓ Ro5 ✓ Clean c1cc(nc(c1)Cl)C(C#N)c2ccc(cc2)Cl
AAN
1AJN
P06875 181.1 Da LogP 1.22 TPSA 80.4 ✓ Ro5 ✓ Clean c1cc(ccc1CC(=O)O)[N+](=O)[O-]
B0S
4M1J
Q9I194 228.2 Da LogP 3.77 TPSA 40.5 ✓ Ro5 ✓ Clean B(CCCCCCCCCCCCC)(O)O
BUB
4WKT
Q9I194 101.9 Da LogP 0.26 TPSA 40.5 ✓ Ro5 ✓ Clean B(CCCC)(O)O
CEN
1JVZ
Q9L5D6 386.4 Da LogP -0.46 TPSA 150.3 ✓ Ro5 ✓ Clean CC(=O)OCC1=C(N2[C@@H]([C@@H](C2=O)NC(=O)CCCC(=O…
DAO
2WYB
Q9I194 200.3 Da LogP 3.99 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCCCCCCCCC(=O)O
DHY
1AI4
P06875 168.1 Da LogP 0.72 TPSA 77.8 ✓ Ro5 Alert c1cc(c(cc1CC(=O)O)O)O
GRO
1K5S
P06875 150.2 Da LogP 1.87 TPSA 37.3 ✓ Ro5 ✓ Clean C[C@H](c1ccccc1)C(=O)O
GUA
1JW0
Q9L5D6 132.1 Da LogP 0.33 TPSA 74.6 ✓ Ro5 ✓ Clean C(CC(=O)O)CC(=O)O
IPH
1AI7
P06875 94.1 Da LogP 1.39 TPSA 20.2 ✓ Ro5 ✓ Clean c1ccc(cc1)O
MNP
1AI5
P06875 181.1 Da LogP 1.22 TPSA 80.4 ✓ Ro5 ✓ Clean c1cc(cc(c1)[N+](=O)[O-])CC(=O)O
MYR
3L94
Q9I194 228.4 Da LogP 4.77 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCCCCCCCCCCC(=O)O
OCA
3L91
Q9I194 144.2 Da LogP 2.43 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCCCCC(=O)O
OMD
1AJP
P06875 168.1 Da LogP 0.72 TPSA 77.8 ✓ Ro5 ✓ Clean c1cc(c(cc1O)CC(=O)O)O
PAC
1FXH
P06875 136.1 Da LogP 1.31 TPSA 37.3 ✓ Ro5 ✓ Clean c1ccc(cc1)CC(=O)O
PMS
1PNM
P06875 172.2 Da LogP 1.07 TPSA 54.4 ✓ Ro5 ✓ Clean c1ccc(cc1)CS(=O)(=O)O
PNN
1FXV
P06875 334.4 Da LogP 0.86 TPSA 86.7 ✓ Ro5 ✓ Clean CC1([C@@H](N2[C@H](S1)[C@@H](C2=O)NC(=O)Cc3cccc…
SOX
1GM8
P06875 352.4 Da LogP 0.60 TPSA 106.9 ✓ Ro5 ✓ Clean CC1([C@@H](N2[C@H]([S@H]1O)[C@@H](C2=O)NC(=O)Cc…
SPA
1AJQ
P06875 142.2 Da LogP 1.38 TPSA 37.3 ✓ Ro5 ✓ Clean c1cc(sc1)CC(=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.