Research workbench
Crystal structure of the R2 subunit of ribonucleotide reductase from chlamydia trachomatis
Analyse Crystal structure of the R2 subunit of ribonucleotide reductase from chlamydia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SYY
- Type
- protein
- Length
- 317 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleoside-diphosphate reductase beta chain
- EC
- 1.17.4.1
- UniProt
- O84835
- Ligands
- FE, PB
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonucleoside-diphosphate reductase beta chain (EC 1.17.4.1) | protein | 317 | 72% helix, 1% strand | O84835 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.34 | 0.77 | 12 | empty |
Compared structures
- 1SYY · Crystal structure of the R2 subunit of ribonucleotide reductase from Chlamydia trachomatis · the same entry in another collection · chain A against A, TM-score 1.00
- O84835 · AlphaFold monomer V2.0 prediction for ribonucleoside-diphosphate reductase subunit beta… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O84835
- Elsewhere: RCSB PDB 1SYY · PDBe 1SYY · UniProt O84835
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