Research workbench
Structure of ribonucleotide reductase R2 from escherichia COLI collected by femtosecond serial crystallography on a coc membrane
Analyse Structure of ribonucleotide reductase R2 from escherichia COLI collected by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BET
- Type
- protein
- Length
- 339 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleoside-diphosphate reductase 1 subunit beta
- EC
- 1.17.4.1
- UniProt
- P69924
- Ligands
- FE
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonucleoside-diphosphate reductase 1 subunit beta (EC 1.17.4.1) | protein | 339 | 70% helix, 4% strand | P69924 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7BET · Structure of Ribonucleotide reductase R2 from Escherichia coli collected by femtosecond… · the same entry in another collection · chain A 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 P69924
- Elsewhere: RCSB PDB 7BET · PDBe 7BET · UniProt P69924
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