Protein profile

KP13_03683

Ubiquinol oxidase subunit 2

Genome: KpKP13

Gene: cyoA AHE46023.1 Structure source: AlphaFold + ColabFold UniProt A0A2X3GWK0

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Amino acids 314

Annotations 8

Features 41

PDB binders 5

Druggability 0.468

Overview

Basic information about this protein and its source genome.

Accession: KP13_03683
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: cyoA AHE46023.1
Status: annotated
Amino acids: 314
Structure source: AlphaFold + ColabFold

GO:0022900 A process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors. GO:0016682 Catalysis of an oxidation-reduction (redox) reaction in which a diphenol, or related compound, acts as a hydrogen or electron donor and reduces oxygen. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0004129 Catalysis of the reaction: 4 Fe(II)-[cytochrome c] + O2 + 8 H+(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H+(out). GO:0009486 Catalysis of the reaction: 2 ubiquinol + O2 + 4 H+ = 2 ubiquinone + 2 H2O + 4 H+ [periplasmic space]. GO:0005507 Binding to a copper (Cu) ion.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 54.317
DEG E-value: 9.88e-113
Localization: CytoplasmicMembrane
ColabFold pLDDT: 81.54

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 0.468

Structure A0A2X3GWK0

Pocket Pocket 23

P2Rank

Structure A0A2X3GWK0

Pocket No pockets

ColabFold model

FPocket 0.423 · Pocket 18

P2Rank 0.013 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 147 / 4744 genomes with a hit

Normalized 0.031

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

GO:0022900 A process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors.
GO:0016682 Catalysis of an oxidation-reduction (redox) reaction in which a diphenol, or related compound, acts as a hydrogen or electron donor and reduces oxygen.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0004129 Catalysis of the reaction: 4 Fe(II)-[cytochrome c] + O2 + 8 H+(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H+(out).
GO:0009486 Catalysis of the reaction: 2 ubiquinol + O2 + 4 H+ = 2 ubiquinone + 2 H2O + 4 H+ [periplasmic space].
GO:0005507 Binding to a copper (Cu) ion.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0042773 The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP.

Sequence Features

Domain/signature hits from InterPro and related databases.

41 records

Show feature table

Start	End	DB	Term	Name
45	67	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
122	282	SUPERFAMILY	SSF49503	Cupredoxins
122	282	InterPro	IPR008972	Cupredoxin
27	112	FunFam	G3DSA:1.10.287.90:FF:000002	Ubiquinol oxidase subunit 2
12	30	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
127	225	CDD	cd04212	CuRO_UO_II
127	225	InterPro	IPR034227	Ubiquinol oxidase subunit 2, cupredoxin domain
27	112	Gene3D	G3DSA:1.10.287.90	-
27	112	InterPro	IPR036257	Cytochrome C oxidase subunit II, transmembrane domain superfamily
149	218	Pfam	PF00116	Cytochrome C oxidase subunit II, periplasmic domain
149	218	InterPro	IPR002429	Cytochrome c oxidase subunit II-like C-terminal
109	314	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	25	ProSiteProfiles	PS51257	Prokaryotic membrane lipoprotein lipid attachment site profile.
286	314	MobiDBLite	mobidb-lite	consensus disorder prediction
239	284	Pfam	PF06481	COX Aromatic Rich Motif
239	284	InterPro	IPR010514	COX aromatic rich motif
10	22	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
28	42	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
43	67	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
14	239	NCBIfam	TIGR01433	ubiquinol oxidase subunit II
14	239	InterPro	IPR006333	Cytochrome o ubiquinol oxidase subunit II
1	312	PIRSF	PIRSF000292	Ubiqnol_oxid_II
1	312	InterPro	IPR006333	Cytochrome o ubiquinol oxidase subunit II
113	282	FunFam	G3DSA:2.60.40.420:FF:000008	Ubiquinol oxidase subunit 2
88	108	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
124	237	ProSiteProfiles	PS50857	Cytochrome oxidase subunit II copper A binding domain profile.
124	237	InterPro	IPR002429	Cytochrome c oxidase subunit II-like C-terminal
68	87	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
29	116	SUPERFAMILY	SSF81464	Cytochrome c oxidase subunit II-like, transmembrane region
29	116	InterPro	IPR036257	Cytochrome C oxidase subunit II, transmembrane domain superfamily
19	242	PANTHER	PTHR22888	CYTOCHROME C OXIDASE, SUBUNIT II
19	242	InterPro	IPR045187	Cytochrome c/quinol oxidase subunit II
21	118	ProSiteProfiles	PS50999	Cytochrome oxidase subunit II transmembrane region profile.
21	118	InterPro	IPR011759	Cytochrome C oxidase subunit II, transmembrane domain
113	282	Gene3D	G3DSA:2.60.40.420	-
113	282	InterPro	IPR008972	Cupredoxin
289	314	MobiDBLite	mobidb-lite	consensus disorder prediction
23	27	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	27	Phobius	SIGNAL_PEPTIDE	Signal peptide region
88	110	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	9	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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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_A0A2X3GWK0	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_03683	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
23				0.468
6				0.226

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
18				0.423

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

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
3PE	6WTI	P0ABJ1	748.1 Da LogP 12.06 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN)OC…`
CUA	1CYX	P0ABJ1	127.1 Da LogP -0.01 TPSA 0.0	✓ Ro5	✓ Clean	`[Cu][Cu]`
HEO	1FFT	P0ABJ1	838.9 Da LogP 8.07 TPSA 110.7	2 viol.	✓ Clean	`Cc1c2cc3[n+]4c(cc5c(c(c6n5[Fe]47n2c(c1CCC(=O)O)…`
U9V	6WTI	P0ABJ1	524.9 Da LogP 10.65 TPSA 52.6	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OCCOC(=O)CCCCCCCCCCCCCC`
UQ8	6WTI	P0ABJ1	727.1 Da LogP 14.40 TPSA 52.6	2 viol.	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)CC=C(C)CC\C=C(/C)\CC…`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC102190506	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC17654239	1.000	314.5 Da LogP 4.79 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCCOC(=O)CCCCCCC`
ZINC27416437	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC1532641	0.972	318.4 Da LogP 4.04 TPSA 52.6	✓ Ro5	Alert	`COC1=C(OC)C(=O)C(C/C=C(\C)CCC=C(C)C)=C(C)C1=O`
ZINC4691823	0.952	258.4 Da LogP 3.23 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCCC(=O)OCCOC(=O)CCCCC`
ZINC100302690	0.875	258.4 Da LogP 4.10 TPSA 35.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OCCOC`
ZINC101034896	0.875	402.6 Da LogP 4.83 TPSA 71.1	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCCOCCOCCOC(=O)CCCCCCC`
ZINC206748657	0.875	374.5 Da LogP 4.05 TPSA 71.1	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCCOCCOCCOC(=O)CCCCC`
ZINC218215426	0.875	402.6 Da LogP 4.83 TPSA 71.1	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)OCCOCCOCCOC(=O)CCCCC`
ZINC1608549	0.870	200.3 Da LogP 3.69 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCCCC`
ZINC1608718	0.870	214.3 Da LogP 4.08 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCCCCC`
ZINC1615264	0.870	214.3 Da LogP 4.08 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCOC(=O)CCCCC`
ZINC1677794	0.870	200.3 Da LogP 3.69 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCC(=O)OCCCCC`
ZINC1684740	0.870	200.3 Da LogP 3.69 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCOC(=O)CCCCC`
ZINC1684760	0.870	228.4 Da LogP 4.47 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCOC(=O)CCCCC`
ZINC1845930	0.870	228.4 Da LogP 4.47 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCOC(=O)CCCCCC`
ZINC2034460	0.870	228.4 Da LogP 4.47 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)OCCCC`
ZINC2039906	0.870	228.4 Da LogP 4.47 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCCCCCC`
ZINC2516185	0.870	214.3 Da LogP 4.08 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)OCCC`
ZINC32147174	0.870	214.3 Da LogP 4.08 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCOC(=O)CCCCCC`
ZINC3875771	0.870	314.5 Da LogP 4.79 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCCCOC(=O)CCCCC(=O)OCCCCCC`
ZINC85590383	0.870	242.4 Da LogP 4.86 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OCCC`
ZINC85936592	0.870	242.4 Da LogP 4.86 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)OCCCCC`
ZINC86022556	0.870	242.4 Da LogP 4.86 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCOC(=O)CCCCCCC`
ZINC5820125	0.833	346.5 Da LogP 3.27 TPSA 71.1	✓ Ro5	✓ Clean	`CCCCCC(=O)OCCOCCOCCOC(=O)CCCCC`
ZINC3875764	0.826	314.5 Da LogP 4.79 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCOC(=O)CCCCCCCCC(=O)OCCCC`
ZINC4100226	0.826	300.4 Da LogP 4.40 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCOC(=O)CCCCCCCC(=O)OCCCC`
ZINC4410479	0.826	286.4 Da LogP 4.01 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCCC(=O)OCCCCOC(=O)CCCCC`
ZINC4721921	0.826	272.4 Da LogP 3.62 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCOC(=O)CCCCCC(=O)OCCCC`
ZINC1848564	0.808	230.3 Da LogP 3.32 TPSA 35.5	✓ Ro5	✓ Clean	`CCCCCCC(=O)OCCOCCCC`
ZINC4429686	0.808	274.4 Da LogP 3.33 TPSA 44.8	✓ Ro5	✓ Clean	`CCCCCCC(=O)OCCOCCOCCCC`
ZINC100036663	0.800	272.4 Da LogP 4.22 TPSA 46.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OCCO`
ZINC138343271	0.800	230.3 Da LogP 3.05 TPSA 46.5	✓ Ro5	✓ Clean	`CCCCCCCCCCC(=O)OCCO`
ZINC77871962	0.800	244.4 Da LogP 3.44 TPSA 46.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OCCO`
ZINC78062261	0.800	243.4 Da LogP 3.41 TPSA 52.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OCCN`
ZINC104333637	0.792	242.4 Da LogP 4.86 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCCCOC(=O)CCCC`
ZINC1584002	0.792	200.3 Da LogP 3.69 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCOC(=O)CCCC`
ZINC1584009	0.792	214.3 Da LogP 4.08 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCOC(=O)CCCC`
ZINC1682726	0.783	244.3 Da LogP 2.84 TPSA 52.6	✓ Ro5	✓ Clean	`CCCOC(=O)CCCCCC(=O)OCCC`
ZINC3875751	0.783	258.4 Da LogP 3.23 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCOC(=O)CCCCC(=O)OCCCC`
ZINC4722486	0.783	272.4 Da LogP 3.62 TPSA 52.6	✓ Ro5	✓ Clean	`CCCOC(=O)CCCCCCCC(=O)OCCC`
ZINC13544781	0.771	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC13544783	0.771	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC100300463	0.769	232.4 Da LogP 3.60 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)OCCS`
ZINC1566534	0.769	216.3 Da LogP 2.93 TPSA 35.5	✓ Ro5	✓ Clean	`CCCCCC(=O)OCCOCCCC`
ZINC4430035	0.769	260.4 Da LogP 2.94 TPSA 44.8	✓ Ro5	✓ Clean	`CCCCCC(=O)OCCOCCOCCCC`
ZINC4977298	0.769	402.6 Da LogP 4.83 TPSA 71.1	✓ Ro5	✓ Clean	`CCCCOCCOC(=O)CCCCCCCCC(=O)OCCOCCCC`
ZINC1648324	0.750	200.3 Da LogP 3.69 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)OCC`

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.