Research workbench
Xprtase from E. COLI
Analyse Xprtase from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NUL
- Type
- protein
- Length
- 278 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Xanthine-guanine phosphoribosyltransferase
- EC
- 2.4.2.22
- UniProt
- P0A9M5
- Ligands
- MG, SO4
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xanthine-guanine phosphoribosyltransferase (EC 2.4.2.22) | protein | 142 | 32% helix, 30% strand | P0A9M5 |
| B | Xanthine-guanine phosphoribosyltransferase (EC 2.4.2.22) | protein | 136 | 30% helix, 26% strand | P0A9M5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.46 | 0.75 | 31 | SO4, MG |
| 2 | 66 | 0.29 | 0.74 | 19 | MG |
Interfaces
1 interface between chains.
- A–B · 1359 Ų buried · 27 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 P0A9M5
- Elsewhere: RCSB PDB 1NUL · PDBe 1NUL · UniProt P0A9M5
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