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Structure analysis of full-length mouse BCS1 complex

Analyse Structure analysis of full-length mouse BCS1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UKO
Type: protein
Length: 2,597 residues
Chains: 7
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9CZP5
Ligands: ADP, MG

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G	—	protein	371	—	Q9CZP5

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 7 copies · chains A, B, C, D, E, F, G
MG · Magnesium ion · metal · 7 copies · chains A, B, C, D, E, F, G

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6UKO · Structure analysis of full-length mouse bcs1 complex · the same entry in another collection · chain G against G, TM-score 1.00
Q9CZP5 · AlphaFold monomer V2.0 prediction for mitochondrial chaperone BCS1 (Q9CZP5) · a predicted model of the same protein · chain D against A, TM-score 0.76

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 Q9CZP5
Elsewhere: RCSB PDB 6UKO · PDBe 6UKO · UniProt Q9CZP5

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