Research workbench
Cobalt substitution of mouse R2 ribonucleotide reductase to model the reactive diferrous state
Analyse Cobalt substitution of mouse R2 ribonucleotide reductase to model the reactive… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H0N
- Type
- protein
- Length
- 288 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11157
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 288 | — | P11157 |
Compared structures
- 1H0N · Cobalt substitution of mouse R2 ribonucleotide reductase to model the reactive diferrous… · the same entry in another collection · chain A against A, TM-score 1.00
- P11157 · AlphaFold monomer V2.0 prediction for ribonucleoside-diphosphate reductase subunit M2… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P11157
- Elsewhere: RCSB PDB 1H0N · PDBe 1H0N · UniProt P11157
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