MolNFT v1 · #169728 · protein
Full-length HSC82 in complex with AHA1 ctd in the presence of amppnp
6XLD: “Full-length HSC82 in complex with AHA1 ctd in the presence of amppnp”. Electron microscopy, 2 ligands (ANP, MG). MolNFT v1 #169728 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6XLD
- Type
- protein
- Length
- 1,349 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P15108, Q12449
- Ligands
- ANP, MG
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 606 | — | P15108 |
| B | — | protein | 604 | — | P15108 |
| C | — | protein | 139 | — | Q12449 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6XLD · Full-length Hsc82 in complex with Aha1 CTD in the presence of AMPPNP · the same entry in another collection · chain B against B, TM-score 1.00
- Q12449 · AlphaFold monomer V2.0 prediction for HSP90 co-chaperone AHA1 (Q12449) · a predicted model of the same protein · chain C against A, TM-score 0.98
- P15108 · AlphaFold monomer V2.0 prediction for ATP-dependent molecular chaperone HSC82 (P15108) · 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 P15108
- Every structure of UniProt Q12449
- Elsewhere: RCSB PDB 6XLD · PDBe 6XLD · UniProt P15108 · UniProt Q12449
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