MolNFT v1 · #169712 · protein
R. capsulatus CIII2CIV bipartite super-complex (sc-2A) with CCOH/CY
6XKW: “R. capsulatus CIII2CIV bipartite super-complex (sc-2A) with CCOH/CY”. Electron microscopy, 3 ligands (HEC, FES, CU). MolNFT v1 #169712 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6XKW
- Type
- protein
- Length
- 2,648 residues
- Chains
- 11
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D5ARP4, D5ARP5, D5ARP7, D5ARP9, Q05389, D5ANZ2, D5ANZ3, D5ANZ4
- Ligands
- HEC, FES, CU
Structure
electron microscopy · 8 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| n | — | protein | 471 | — | D5ARP4 |
| o | — | protein | 190 | — | D5ARP5 |
| p | — | protein | 254 | — | D5ARP7 |
| h | — | protein | 25 | — | D5ARP9 |
| Y | — | protein | 30 | — | Q05389 |
| E, R | — | protein | 181 | — | D5ANZ2 |
| C, P | — | protein | 423 | — | D5ANZ3 |
| D, Q | — | protein | 235 | — | D5ANZ4 |
Ligands and binding sites
- HEC · Heme C · ligand · 11 copies · chains n, o, p, C, D, P, Q
- FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains E, R
- CU · Copper (II) ion · metal · chains n
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 D5ARP4
- Every structure of UniProt D5ARP5
- Every structure of UniProt D5ARP7
- Every structure of UniProt D5ARP9
- Every structure of UniProt Q05389
- Every structure of UniProt D5ANZ2
- Every structure of UniProt D5ANZ3
- Every structure of UniProt D5ANZ4
- Elsewhere: RCSB PDB 6XKW · PDBe 6XKW · UniProt D5ARP4 · UniProt D5ARP5 · UniProt D5ARP7 · UniProt D5ARP9 · UniProt Q05389 · UniProt D5ANZ2 · UniProt D5ANZ3 · UniProt D5ANZ4
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