Protein profile

KP13_02339

Cobalt import ATP-binding protein CbiO

Genome: KpKP13

Gene: cbiO AHE42909.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GWY5
Export view
Amino acids 274
Annotations 7
Features 18
PDB binders 3
Druggability 0.245

Overview

Basic information about this protein and its source genome.

Accession
KP13_02339
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
cbiO AHE42909.1
Status
annotated
Amino acids
274
Structure source
AlphaFold + ColabFold
GO
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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0006824 The directed movement of cobalt (Co2+) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
33.898
Human E-value
4.16e-13
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
42.222
DEG E-value
0.033
Localization
CytoplasmicMembrane
ColabFold pLDDT
93.8

Selected Druggability evidence

AlphaFold / UniProt model

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 0.245
Structure A0A0H3GWY5
Pocket Pocket 21
P2Rank 0.371
Structure A0A0H3GWY5
Pocket Pocket 1
ColabFold model
FPocket 0.151 · Pocket 23
P2Rank 0.193 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 52 / 4744 genomes with a hit
Normalized 0.011

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

7
  • 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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0006824 The directed movement of cobalt (Co2+) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
  • GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
  • 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: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.

Sequence Features

Domain/signature hits from InterPro and related databases.

18 records
Show feature table
Start End DB Term Name
26 212 SMART SM00382 AAA_5
26 212 InterPro IPR003593 AAA+ ATPase domain
17 165 Pfam PF00005 ABC transporter
17 165 InterPro IPR003439 ABC transporter-like, ATP-binding domain
1 257 Gene3D G3DSA:3.40.50.300 -
1 257 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
11 199 NCBIfam TIGR01166 cobalt ABC transporter, ATP-binding protein
11 199 InterPro IPR005876 Cobalt transport protein ATP-binding subunit
2 236 ProSiteProfiles PS50893 ATP-binding cassette, ABC transporter-type domain profile.
2 236 InterPro IPR003439 ABC transporter-like, ATP-binding domain
1 261 FunFam G3DSA:3.40.50.300:FF:000224 Energy-coupling factor transporter ATP-binding protein EcfA
3 230 SUPERFAMILY SSF52540 P-loop containing nucleoside triphosphate hydrolases
3 230 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
6 213 CDD cd03225 ABC_cobalt_CbiO_domain1
6 213 InterPro IPR015856 ABC transporter, CbiO/EcfA subunit
137 151 ProSitePatterns PS00211 ABC transporters family signature.
137 151 InterPro IPR017871 ABC transporter-like, conserved site
4 247 PANTHER PTHR43553 HEAVY METAL TRANSPORTER

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

Loading 3D structure...

Legend High Medium Low

Structural evidence

0 + 2

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GWY5
AlphaFold — — full sequence — Viewing
ColabFold KP13_02339
ColabFold — — 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
21 0.245
8 0.238

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 4.3 0.178
2 3.05 0.101
3 0.9 0.004

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
ACP
5X40
O68106 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)…
ANP
5D3M
Q1GBI9 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)…
LMT
6ZG3
Q1GBI9 510.6 Da LogP -0.45 TPSA 178.5 3 viol. ✓ Clean CCCCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1…

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.