Protein profile

PA2397

pyoverdine biosynthesis protein PvdE

Genome: NC_002516.2

Gene: pvdE PA2397 Structure source: AlphaFold UniProt Q9I183
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Amino acids 549
Annotations 10
Features 44
PDB binders 3
Druggability 0.874

Overview

Basic information about this protein and its source genome.

Accession
PA2397
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
pvdE PA2397
Status
annotated
Amino acids
549
Structure source
AlphaFold
GO
GO:0043190 A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter. GO:0140359 Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. GO:0042626 Primary active transporter of a solute across a membrane, via the reaction: ATP + H2O = ADP + phosphate, to directly drive the transport of a substance across a membrane. The transport protein may be transiently phosphorylated (P-type transporters), or not (ABC-type transporters and other families of transporters). Primary active transport occurs up the solute's concentration gradient and is driven by a primary energy source. GO:1904680 Enables the transfer of a peptide from one side of a membrane to the other.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
33.333
Human E-value
1.31e-12
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 0.874
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

10 GO

Gene Ontology (GO)

10
  • GO:0043190 A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter.
  • GO:0140359 Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
  • GO:0042626 Primary active transporter of a solute across a membrane, via the reaction: ATP + H2O = ADP + phosphate, to directly drive the transport of a substance across a membrane. The transport protein may be transiently phosphorylated (P-type transporters), or not (ABC-type transporters and other families of transporters). Primary active transport occurs up the solute's concentration gradient and is driven by a primary energy source.
  • GO:1904680 Enables the transfer of a peptide from one side of a membrane to the other.
  • GO:0015833 The directed movement of peptides, compounds of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
  • GO:0002049 The chemical reactions and pathways resulting in the formation of the siderochrome pyoverdine.
  • GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.

Sequence Features

Domain/signature hits from InterPro and related databases.

44 records
Show feature table
Start End DB Term Name
298 549 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
40 546 PANTHER PTHR24221 ATP-BINDING CASSETTE SUB-FAMILY B
40 546 InterPro IPR039421 Type 1 protein exporter
43 61 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
62 83 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
21 299 ProSiteProfiles PS50929 ABC transporter integral membrane type-1 fused domain profile.
21 299 InterPro IPR011527 ABC transporter type 1, transmembrane domain
2 314 FunFam G3DSA:1.20.1560.10:FF:000219 Pyoverdine biosynthesis protein PvdE
276 298 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
129 151 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
152 156 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
176 238 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
324 549 FunFam G3DSA:3.40.50.300:FF:001035 ABC transporter ATP-binding protein YojI
157 175 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
358 492 Pfam PF00005 ABC transporter
358 492 InterPro IPR003439 ABC transporter-like, ATP-binding domain
266 270 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
239 261 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
324 548 Gene3D G3DSA:3.40.50.300 -
324 548 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
10 312 SUPERFAMILY SSF90123 ABC transporter transmembrane region
10 312 InterPro IPR036640 ABC transporter type 1, transmembrane domain superfamily
129 151 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
84 128 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
336 545 SUPERFAMILY SSF52540 P-loop containing nucleoside triphosphate hydrolases
336 545 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
2 314 Gene3D G3DSA:1.20.1560.10 ABC transporter type 1, transmembrane domain
2 314 InterPro IPR036640 ABC transporter type 1, transmembrane domain superfamily
336 549 ProSiteProfiles PS50893 ATP-binding cassette, ABC transporter-type domain profile.
336 549 InterPro IPR003439 ABC transporter-like, ATP-binding domain
336 541 CDD cd03228 ABCC_MRP_Like
21 42 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
5 549 NCBIfam TIGR01194 cyclic peptide export ABC transporter
5 549 InterPro IPR005898 Cyclic peptide transporter SyrD/Yoji-like
1 20 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
21 43 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
365 548 SMART SM00382 AAA_5
365 548 InterPro IPR003593 AAA+ ATPase domain
53 75 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
271 297 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
239 265 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
155 177 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
22 174 Pfam PF00664 ABC transporter transmembrane region
22 174 InterPro IPR011527 ABC transporter type 1, transmembrane domain

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

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Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA2397
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 0.874
10 0.581
4 0.211

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.

53 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
AGS
4S0F
A3DCU1 523.2 Da LogP -1.51 TPSA 262.1 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
ANP
3B60
P63359 506.2 Da LogP -2.06 TPSA 281.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
DMU
6TEJ
A0A100XE85 482.6 Da LogP -1.23 TPSA 178.5 2 viol. ✓ Clean CCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1)C…

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.