Research workbench
Combined crystallographic refinement and energy minimization of rubredoxin at 1.2 ångström resolution
Analyse Combined crystallographic refinement and energy minimization of rubredoxin at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5RXN
- Type
- protein
- Length
- 54 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rubredoxin
- UniProt
- P00268
- Ligands
- FE
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rubredoxin | protein | 54 | 17% helix, 22% strand | P00268 |
Ligands and binding sites
- FE · Fe (III) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5RXN · Combined crystallographic refinement and energy minimization of rubredoxin at 1.2… · the same entry in another collection · chain A against A, TM-score 1.00
- P00268 · AlphaFold monomer V2.0 prediction for rubredoxin (P00268) · a predicted model of the same protein · chain A 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 P00268
- Elsewhere: RCSB PDB 5RXN · PDBe 5RXN · UniProt P00268
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