Protein profile

PA2305

protein AmbB

Genome: NC_002516.2

Gene: ambB PA2305 Structure source: Experimental + AlphaFold UniProt Q9I1H0
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Amino acids 1249
Annotations 9
Features 38
PDB binders 14
Druggability 0.786

Overview

Basic information about this protein and its source genome.

Accession
PA2305
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
ambB PA2305
Status
annotated
Amino acids
1249
Structure source
Experimental + AlphaFold
EC
6.2.1.67
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0009366 A multienzyme complex usually composed of four proteins, EntB, EntD, EntE and EntF. Plays a role in the enterobactin biosynthesis pathway. GO:0047527 Catalysis of the reaction: ATP + 2,3-dihydroxybenzoate + L-serine = products of ATP breakdown + N-(2,3-dihydroxybenzoyl)-L-serine. GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate). GO:0043041 Activation of an amino acid for incorporation into a peptide by a nonribosomal process.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
33.557
Human E-value
1.33e-12
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Unknown

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 0.786
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0009366 A multienzyme complex usually composed of four proteins, EntB, EntD, EntE and EntF. Plays a role in the enterobactin biosynthesis pathway.
  • GO:0047527 Catalysis of the reaction: ATP + 2,3-dihydroxybenzoate + L-serine = products of ATP breakdown + N-(2,3-dihydroxybenzoyl)-L-serine.
  • GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate).
  • GO:0043041 Activation of an amino acid for incorporation into a peptide by a nonribosomal process.
  • GO:0009239 The chemical reactions and pathways resulting in the formation of enterobactin, a catechol-derived siderochrome of Enterobacteria; enterobactin (N',N',N''-(2,6,10-trioxo-1,5,9-triacyclodecane-3,7,11-triyl)tris(2,3-dihydroxy)benzamide) is a self-triester of 2,3-dihydroxy-N-benzoyl-L-serine and a product of the shikimate pathway.
  • 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.

38 records
Show feature table
Start End DB Term Name
629 725 Gene3D G3DSA:3.30.300.30 -
629 725 InterPro IPR045851 AMP-binding enzyme, C-terminal domain superfamily
116 136 Coils Coil Coil
267 400 Gene3D G3DSA:3.40.50.980 -
266 657 NCBIfam TIGR01733 amino acid adenylation domain
266 657 InterPro IPR010071 Amino acid adenylation domain
763 778 ProSitePatterns PS00012 Phosphopantetheine attachment site.
763 778 InterPro IPR006162 Phosphopantetheine attachment site
549 624 Gene3D G3DSA:2.30.38.10 Luciferase; Domain 3
628 729 FunFam G3DSA:3.30.300.30:FF:000010 Enterobactin synthetase component F
267 400 FunFam G3DSA:3.40.50.980:FF:000001 Non-ribosomal peptide synthetase
824 977 SUPERFAMILY SSF52777 CoA-dependent acyltransferases
241 721 CDD cd12115 A_NRPS_Sfm_like
823 1150 Pfam PF00668 Condensation domain
823 1150 InterPro IPR001242 Condensation domain
824 1184 Gene3D G3DSA:3.30.559.10 -
824 1184 InterPro IPR023213 Chloramphenicol acetyltransferase-like domain superfamily
189 1151 PANTHER PTHR45527 NONRIBOSOMAL PEPTIDE SYNTHETASE
742 804 Pfam PF00550 Phosphopantetheine attachment site
742 804 InterPro IPR009081 Phosphopantetheine binding ACP domain
735 823 SUPERFAMILY SSF47336 ACP-like
735 823 InterPro IPR036736 ACP-like superfamily
997 1231 Gene3D G3DSA:3.30.559.30 Nonribosomal peptide synthetase, condensation domain
734 809 ProSiteProfiles PS50075 Carrier protein (CP) domain profile.
734 809 InterPro IPR009081 Phosphopantetheine binding ACP domain
857 877 Coils Coil Coil
249 548 Gene3D G3DSA:3.40.50.980 -
385 396 ProSitePatterns PS00455 Putative AMP-binding domain signature.
385 396 InterPro IPR020845 AMP-binding, conserved site
726 812 Gene3D G3DSA:1.10.1200.10 -
726 812 InterPro IPR036736 ACP-like superfamily
245 633 Pfam PF00501 AMP-binding enzyme
245 633 InterPro IPR000873 AMP-dependent synthetase/ligase domain
716 741 MobiDBLite mobidb-lite consensus disorder prediction
208 752 SUPERFAMILY SSF56801 Acetyl-CoA synthetase-like
642 715 Pfam PF13193 AMP-binding enzyme C-terminal domain
642 715 InterPro IPR025110 AMP-binding enzyme, C-terminal domain
1004 1236 SUPERFAMILY SSF52777 CoA-dependent acyltransferases

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

3 + 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 7X0E
X-ray 2.10 Å A
41.9% 727-1249
PDBe RCSB PDBj File
Viewing
PDB 7X0F
X-ray 2.20 Å A,B,C,D
41.9% 727-1249
PDBe RCSB PDBj File
Loaded
PDB 7X17
X-ray 2.50 Å A,B,C,D
41.9% 727-1249
PDBe RCSB PDBj File
Loaded
AlphaFold PA2305
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
1 0.786

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 17.23 0.799
2 10.8 0.579
3 2.59 0.074
4 1.68 0.029
5 1.32 0.014

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.

64 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
5FQ
5DUA
Q9Z4X6 158.2 Da LogP 0.64 TPSA 55.1 ✓ Ro5 ✓ Clean CCCCCNC(=O)[C@H](C)N
5S4
5ES8
Q70LM7 440.4 Da LogP -1.80 TPSA 200.3 1 viol. ✓ Clean CC(C)[C@@H](C(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C)(C…
9EF
6MFX
Q70LM7 383.3 Da LogP -1.76 TPSA 174.3 1 viol. ✓ Clean CC(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP(=O)(O)…
APC
5ES7
Q70LM7 505.2 Da LogP -1.52 TPSA 269.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
CO8
7C1R
E5ATN9 893.7 Da LogP 1.03 TPSA 363.6 3 viol. ✓ Clean CCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…
DG9
6MG0
Q70LM7 785.8 Da LogP -2.85 TPSA 336.7 3 viol. ✓ Clean CC(C)[C@H]([C@H](CS(=O)(=O)NC[C@@H]1[C@H]([C@H]…
FGU
7C1S
E5ATN9 232.3 Da LogP 0.76 TPSA 72.2 ✓ Ro5 ✓ Clean CC(C)C[C@@H](C(=O)SCCNC(=O)C)N
FLC
6P1J
A0A0B5H0S3 189.1 Da LogP -5.25 TPSA 140.6 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
FON
5ES7
Q70LM7 473.4 Da LogP -0.73 TPSA 219.8 1 viol. ✓ Clean c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC[C@@H]2…
JQG
6MFW
Q70LM7 468.4 Da LogP -1.84 TPSA 200.2 1 viol. ✓ Clean CC(C)[C@@H](C(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C)(C…
KH4
4PWV
F2YRY5 452.4 Da LogP -0.60 TPSA 190.9 1 viol. ✓ Clean CC(C)(COP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCSC(=O)c…
KIV
6ULZ
Q70LM7 116.1 Da LogP 0.30 TPSA 54.4 ✓ Ro5 ✓ Clean CC(C)C(=O)C(=O)O
PNS
5ES9
Q70LM7 358.4 Da LogP -0.96 TPSA 145.2 1 viol. ✓ Clean CC(C)(COP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCS)O
UM2
5DU9
Q9Z4X6 144.2 Da LogP 0.25 TPSA 55.1 ✓ Ro5 ✓ Clean CCCCNC(=O)[C@H](C)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.