Research workbench
Crystal structure of C-as lyase with mutations Y100H and V102F
Analyse Crystal structure of C-as lyase with mutations Y100H and V102F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DFG
- Type
- protein
- Length
- 116 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE
- UniProt
- D1A230
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE | protein | 116 | 22% helix, 41% strand | D1A230 |
Compared structures
- 5DFG · Crystal structure of C-As lyase with mutations Y100H and V102F · 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 5DFG · PDBe 5DFG · UniProt D1A230
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.