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Crystal structure of C-as lyase with mutation K105E
Analyse Crystal structure of C-as lyase with mutation K105E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XCK
- Type
- protein
- Length
- 219 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE
- UniProt
- D1A230
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE | protein | 109 | 23% helix, 43% strand | D1A230 |
| B | GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE | protein | 110 | 23% helix, 43% strand | D1A230 |
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 | 65 | 0.40 | 0.79 | 14 | empty |
| 2 | 59 | 0.36 | 0.78 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1478 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 6XCK · Crystal structure of C-As lyase with mutation K105E · 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 D1A230
- Elsewhere: RCSB PDB 6XCK · PDBe 6XCK · UniProt D1A230
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