MolNFT v2 · #205009 · protein
Structure of the GroEL-ATP complex plunge-frozen 13 ms after mixing with ATP
8BLY: “Structure of the GroEL-ATP complex plunge-frozen 13 ms after mixing with ATP”. Electron microscopy at 3.2, 2 ligands (ATP, MG). MolNFT v2 #205009 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 8BLY
- Type
- protein
- Length
- 7,322 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.2
- Source
- Escherichia coli
- UniProt
- P0A6F5
- Ligands
- ATP, MG
Structure
electron microscopy · resolution 3.2 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | — | protein | 523 | — | P0A6F5 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 14 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N
- MG · Magnesium ion · metal · 14 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P0A6F5 · AlphaFold monomer V2.0 prediction for 60 kda chaperonin (P0A6F5) · a predicted model of the same protein · chain J 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 P0A6F5
- Elsewhere: RCSB PDB 8BLY · PDBe 8BLY · UniProt P0A6F5
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