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The crystal structure of a GLYOXALASE/BLEOMYCIN resistance protein from streptomyces sp. CB03234
Analyse The crystal structure of a GLYOXALASE/BLEOMYCIN resistance protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UJP
- Type
- protein
- Length
- 228 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GLYOXALASE/BLEOMYCIN resisance PROTEIN/DIOXYGENASE
- UniProt
- A0A125SA29
- Ligands
- CA
- Pockets
- 4 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | GLYOXALASE/BLEOMYCIN resisance PROTEIN/DIOXYGENASE | protein | 114 | 19% helix, 42% strand | A0A125SA29 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 274 | 0.53 | 0.75 | 35 | MES |
| 2 | 244 | 0.53 | 0.76 | 34 | empty |
| 3 | 92 | 0.42 | 0.78 | 18 | empty |
| 4 | 65 | 0.38 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 971 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 5UJP · The crystal structure of a glyoxalase/bleomycin resistance protein from Streptomyces sp.… · the same entry in another collection · chain A against A, 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 A0A125SA29
- Elsewhere: RCSB PDB 5UJP · PDBe 5UJP · UniProt A0A125SA29
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