Research workbench
Crystal structure of C-as lyase with mutations Y100H and V102F (monoclinic form)
Analyse Crystal structure of C-as lyase with mutations Y100H and V102F (monoclinic form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HCW
- Type
- protein
- Length
- 456 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE
- UniProt
- D1A230
- Pockets
- 5 · best druggability 0.67
Structure
x-ray diffraction · 4 distinct chains · 21% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE | protein | 110 | 24% helix, 44% strand | D1A230 |
| B | GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE | protein | 118 | 22% helix, 44% strand | D1A230 |
| C | GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE | protein | 113 | 20% helix, 39% strand | D1A230 |
| D | GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE | protein | 115 | 20% helix, 46% strand | D1A230 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 647 | 0.67 | 0.76 | 98 | empty |
| 2 | 142 | 0.54 | 0.81 | 17 | empty |
| 3 | 79 | 0.45 | 0.81 | 14 | empty |
| 4 | 108 | 0.45 | 0.78 | 14 | empty |
| 5 | 71 | 0.41 | 0.80 | 17 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1496 Ų buried · 18 hydrogen bonds · protein-protein
- C–D · 1449 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 351 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 173 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5HCW · Crystal structure of C-As lyase with mutations Y100H and V102F (monoclinic form) · 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 5HCW · PDBe 5HCW · UniProt D1A230
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