Research workbench
Crystal structure of inosine-uridine preferring nucleoside hydrolase from bacillus anthracis at 2.2A resolution
Analyse Crystal structure of inosine-uridine preferring nucleoside hydrolase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C40
- Type
- protein
- Length
- 602 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inosine-uridine preferring nucleoside hydrolase family protein
- EC
- 3.2.2.1
- UniProt
- Q81QM4
- Ligands
- RIB, CA
- Pockets
- 4 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inosine-uridine preferring nucleoside hydrolase family protein (EC 3.2.2.1) | protein | 302 | 42% helix, 19% strand | Q81QM4 |
| B | Inosine-uridine preferring nucleoside hydrolase family protein (EC 3.2.2.1) | protein | 300 | 43% helix, 18% strand | Q81QM4 |
Ligands and binding sites
- RIB · alpha-D-ribofuranose · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 263 | 0.66 | 0.82 | 24 | CA, RIB |
| 2 | 290 | 0.64 | 0.80 | 32 | RIB |
| 3 | 95 | 0.55 | 0.85 | 21 | empty |
| 4 | 98 | 0.54 | 0.84 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 977 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2C40 · Crystal structure of inosine-uridine preferring nucleoside hydrolase from bacillus… · the same entry in another collection · chain B against B, 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 Q81QM4
- Elsewhere: RCSB PDB 2C40 · PDBe 2C40 · UniProt Q81QM4
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