MolNFT v1 · #166264 · protein
Structure analysis of full-length mouse BCS1 complex
6UKO: “Structure analysis of full-length mouse BCS1 complex”. X-ray diffraction, 2 ligands (ADP, MG). MolNFT v1 #166264 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
- 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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