Research workbench
Human ribonucleotide reductase, subunit M2 B
Analyse Human ribonucleotide reductase, subunit M2 B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VUX
- Type
- protein
- Length
- 527 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleoside-diphosphate reductase subunit M2 B
- EC
- 1.17.4.1
- UniProt
- Q7LG56
- Ligands
- FE
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonucleoside-diphosphate reductase subunit M2 B (EC 1.17.4.1) | protein | 272 | 71% helix, 0% strand | Q7LG56 |
| B | Ribonucleoside-diphosphate reductase subunit M2 B (EC 1.17.4.1) | protein | 255 | 71% helix, 0% strand | Q7LG56 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 672 | 0.75 | 0.80 | 49 | empty |
| 2 | 431 | 0.68 | 0.80 | 44 | empty |
| 3 | 147 | 0.53 | 0.80 | 21 | empty |
| 4 | 138 | 0.51 | 0.80 | 23 | empty |
| 5 | 52 | 0.29 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1383 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
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 Q7LG56
- Elsewhere: RCSB PDB 2VUX · PDBe 2VUX · UniProt Q7LG56
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