Research workbench
Crystal structure of a GLYOXALASE/DIOXYGENASE from nostoc punctiforme
Analyse Crystal structure of a GLYOXALASE/DIOXYGENASE from nostoc punctiforme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KOL
- Type
- protein
- Length
- 146 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE
- UniProt
- B2IY64
- Ligands
- CO
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE | protein | 146 | 20% helix, 29% strand | B2IY64 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 236 | 0.56 | 0.78 | 26 | empty |
| 2 | 75 | 0.41 | 0.79 | 17 | empty |
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 3KOL · Crystal structure of a glyoxalase/dioxygenase from Nostoc punctiforme · 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 B2IY64
- Elsewhere: RCSB PDB 3KOL · PDBe 3KOL · UniProt B2IY64
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