MolNFT v2 · #158245 · protein
ADP-bound human mitochondrial Hsp60-Hsp10 half-football complex
6MRD: “ADP-bound human mitochondrial Hsp60-Hsp10 half-football complex”. Electron microscopy at 3.82, 2 ligands (ADP, MG). MolNFT v2 #158245 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6MRD
- Type
- protein
- Length
- 4,396 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.82
- Source
- Homo sapiens
- UniProt
- P10809, P61604
- Ligands
- ADP, MG
Structure
electron microscopy · resolution 3.82 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, G, F, E, D, C, B | — | protein | 528 | — | P10809 |
| O, U, T, S, R, Q, P | — | protein | 100 | — | P61604 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 7 copies · chains A, G, F, E, D, C, B
- MG · Magnesium ion · metal · 7 copies · chains A, G, F, E, D, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6MRD · ADP-bound human mitochondrial HSP60-HSP10 half-football complex · the same entry in another collection · chain Q against Q, TM-score 1.00
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 P10809
- Every structure of UniProt P61604
- Elsewhere: RCSB PDB 6MRD · PDBe 6MRD · UniProt P10809 · UniProt P61604
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