MolNFT v1 · #2935 · protein
Crystal structure of a reduced, active form of the ni-fe-se hydrogenase from desulfomicrobium baculatum
1CC1: “Crystal structure of a reduced, active form of the ni-fe-se hydrogenase from desulfomicrobium baculatum”. X-ray diffraction. MolNFT v1 #2935 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1CC1
- Type
- protein
- Length
- 762 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P13063, P13065
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| S | — | protein | 275 | — | P13063 |
| L | — | protein | 487 | — | P13065 |
Compared structures
- 1CC1 · Crystal structure of a reduced, active form of the ni-fe-se hydrogenase from… · the same entry in another collection · chain S against S, TM-score 1.00
- P13063 · AlphaFold monomer V2.0 prediction for periplasmic [nifese] hydrogenase small subunit… · a predicted model of the same protein · chain S 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 P13063
- Every structure of UniProt P13065
- Elsewhere: RCSB PDB 1CC1 · PDBe 1CC1 · UniProt P13063 · UniProt P13065
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