Research workbench
Methanococcus maripaludis chaperonin complex in open conformation
Analyse Methanococcus maripaludis chaperonin complex in open conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RAK
- Type
- protein
- Length
- 8,112 residues
- Chains
- 16
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q877G8
- Ligands
- ATP
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| U, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O | — | protein | 507 | — | Q877G8 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 16 copies · chains U, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q877G8
- Elsewhere: RCSB PDB 7RAK · PDBe 7RAK · UniProt Q877G8
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