Research workbench
Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
Analyse Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ISL
- Type
- protein
- Length
- 774 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Purine catabolism protein pucg
- EC
- 2.-.-.-
- UniProt
- O32148
- Ligands
- PLP
- Pockets
- 6 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Purine catabolism protein pucg (EC 2.-.-.-) | protein | 387 | 43% helix, 15% strand | O32148 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 253 | 0.73 | 0.87 | 39 | PLP |
| 2 | 293 | 0.70 | 0.84 | 45 | PLP |
| 3 | 56 | 0.38 | 0.80 | 16 | empty |
| 4 | 51 | 0.37 | 0.80 | 16 | empty |
| 5 | 64 | 0.31 | 0.75 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 2854 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 3ISL · Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucG) from Bacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- O32148 · AlphaFold monomer V2.0 prediction for (S)-ureidoglycine--glyoxylate transaminase (O32148) · 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 O32148
- Elsewhere: RCSB PDB 3ISL · PDBe 3ISL · UniProt O32148
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