Research workbench
cobalt-substituted rubredoxin
Analyse cobalt-substituted rubredoxin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R0H
- Type
- protein
- Length
- 53 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.7
- Source
- Clostridium pasteurianum
- Molecule
- Rubredoxin
- UniProt
- P00268
- Ligands
- CO
Structure
x-ray diffraction · resolution 1.7 · 1 distinct chain · 17% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rubredoxin | protein | 53 | 17% helix, 23% strand | P00268 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 P00268
- Elsewhere: RCSB PDB 1R0H · PDBe 1R0H · UniProt P00268
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