Research workbench
Crystal structure of hypothetical protein BH1468 from bacillus halodurans C-125
Analyse Crystal structure of hypothetical protein BH1468 from bacillus halodurans C-125 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OA4
- Type
- protein
- Length
- 138 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glyoxalase
- UniProt
- Q9KCV1
- Ligands
- ZN, SO4
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glyoxalase | protein | 138 | 28% helix, 38% strand | Q9KCV1 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 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 | 129 | 0.62 | 0.86 | 29 | GOL |
| 2 | 60 | 0.28 | 0.74 | 13 | empty |
Compared structures
- 3OA4 · CRYSTAL STRUCTURE OF hypothetical protein BH1468 from Bacillus halodurans C-125 · 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 Q9KCV1
- Elsewhere: RCSB PDB 3OA4 · PDBe 3OA4 · UniProt Q9KCV1
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