Research workbench
Structure of ribonucleotide reductase protein R1
Analyse Structure of ribonucleotide reductase protein R1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RLR
- Type
- protein
- Length
- 737 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleotide reductase protein R1
- EC
- 1.17.4.1
- UniProt
- P00452
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonucleotide reductase protein R1 (EC 1.17.4.1) | protein | 737 | 47% helix, 11% strand | P00452 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 602 | 0.70 | 0.79 | 82 | empty |
| 2 | 192 | 0.47 | 0.75 | 25 | empty |
| 3 | 93 | 0.40 | 0.77 | 21 | empty |
| 4 | 67 | 0.39 | 0.79 | 23 | empty |
| 5 | 102 | 0.35 | 0.74 | 21 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P00452
- Elsewhere: RCSB PDB 1RLR · PDBe 1RLR · UniProt P00452
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