Research workbench
Ribonucleotide reductase R2 protein from aquifex aeolicus
Analyse Ribonucleotide reductase R2 protein from aquifex aeolicus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AIK
- Type
- protein
- Length
- 321 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleoside-diphosphate reductase subunit beta, ribonucleoside-diphosphate reductase…
- EC
- 1.17.4.1
- UniProt
- O67475
- Ligands
- FE2
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonucleoside-diphosphate reductase subunit beta, ribonucleoside-diphosphate reductase subunit beta (EC 1.17.4.1) | protein | 321 | 70% helix, 1% strand | O67475 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7AIK · Ribonucleotide Reductase R2 protein from Aquifex aeolicus · the same entry in another collection · chain A against A, TM-score 1.00
- O67475 · AlphaFold monomer V2.0 prediction for ribonucleoside-diphosphate reductase subunit beta… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O67475
- Elsewhere: RCSB PDB 7AIK · PDBe 7AIK · UniProt O67475
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