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Mitochondrial outer membrane protein

Analyse Mitochondrial outer membrane protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EKM
Type: protein
Length: 1,162 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.6
Source: Homo sapiens
Molecule: ATP-binding cassette sub-family B member 6, mitochondrial
UniProt: Q9NP58
Pockets: 10 · best druggability 0.84

Structure

electron microscopy · resolution 3.6 · 1 distinct chain · 38% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	ATP-binding cassette sub-family B member 6, mitochondrial	protein	581	38% helix, 10% strand	Q9NP58

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1167	0.84	0.85	103	empty
2	181	0.64	0.84	29	empty
3	187	0.64	0.84	37	empty
4	168	0.63	0.84	38	empty
5	274	0.63	0.80	29	empty

Interfaces

1 interface between chains.

A–B · 6124 Å² buried · 36 hydrogen bonds · protein-protein

Compared structures

7EKM · Mitochondrial outer membrane protein · the same entry in another collection · chain A against A, TM-score 1.00
Q9NP58 · AlphaFold monomer V2.0 prediction for ATP-binding cassette sub-family B member 6… · a predicted model of the same protein · chain B against A, TM-score 0.90

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9NP58
Elsewhere: RCSB PDB 7EKM · PDBe 7EKM · UniProt Q9NP58

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