MolNFT v1 · #121079 · protein
Caldalaklibacillus thermarum F1-ATPase (wild type)
5HKK: “Caldalaklibacillus thermarum F1-ATPase (wild type)”. X-ray diffraction. MolNFT v1 #121079 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5HKK
- Type
- protein
- Length
- 6,451 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- F5LA74, F5LA72, F5LA73, F5LA71
Structure
x-ray diffraction · 8 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 475 | — | F5LA74 |
| B, J | — | protein | 475 | — | F5LA74 |
| C | — | protein | 476 | — | F5LA74 |
| D, E, F, L, M, N | — | protein | 461 | — | F5LA72 |
| G, O | — | protein | 284 | — | F5LA73 |
| H, P | — | protein | 132 | — | F5LA71 |
| I | — | protein | 474 | — | F5LA74 |
| K | — | protein | 478 | — | F5LA74 |
Compared structures
- 5HKK · Caldalaklibacillus thermarum F1-ATPase (wild type) · the same entry in another collection · chain A against A, 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 F5LA74
- Every structure of UniProt F5LA72
- Every structure of UniProt F5LA73
- Every structure of UniProt F5LA71
- Elsewhere: RCSB PDB 5HKK · PDBe 5HKK · UniProt F5LA74 · UniProt F5LA72 · UniProt F5LA73 · UniProt F5LA71
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