MolNFT v1 · #31164 · protein
Ribonucleotide reductase R2 from escherichia COLI in space group P6(1)22
2ALX · Ribonucleoside-diphosphate reductase 1: “Ribonucleotide reductase R2 from escherichia COLI in space group P6(1)22”. X-ray diffraction, 2 ligands (HG, MN). MolNFT v1 #31164 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2ALX
- Type
- protein
- Length
- 339 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleoside-diphosphate reductase 1
- EC
- 1.17.4.1
- UniProt
- P69924
- Ligands
- HG, MN
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonucleoside-diphosphate reductase 1 (EC 1.17.4.1) | protein | 339 | 71% helix, 4% strand | P69924 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 4 copies · chains A
- MN · Manganese (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2ALX · Ribonucleotide Reductase R2 from Escherichia coli in space group P6(1)22 · 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 2ALX · PDBe 2ALX · UniProt P69924
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