Research workbench
Bimetallic dodecameric cage design 1 (BMC1) from cytochrome CB562
Analyse Bimetallic dodecameric cage design 1 (BMC1) from cytochrome CB562 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OT9
- Type
- protein
- Length
- 424 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0ABE7
- Ligands
- HAE, HEC, ZN, FE
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, D, B, A | — | protein | 106 | — | P0ABE7 |
Ligands and binding sites
- HAE · Acetohydroxamic acid · ligand · 4 copies · chains C, A, D, B
- HEC · Heme C · ligand · 4 copies · chains C, D, B, A
- ZN · Zinc ion · metal · 6 copies · chains C, D, A, B
- FE · Fe (III) ion · metal · 2 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6OT9 · Bimetallic dodecameric cage design 1 (BMC1) from cytochrome cb562 · the same entry in another collection · chain A against A, TM-score 1.00
- P0ABE7 · AlphaFold monomer V2.0 prediction for soluble cytochrome B562 (P0ABE7) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P0ABE7
- Elsewhere: RCSB PDB 6OT9 · PDBe 6OT9 · UniProt P0ABE7
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