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Crystal structure of arsi C-as lyase solved by ni-sad phasing
Analyse Crystal structure of arsi C-as lyase solved by ni-sad phasing in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5C4P
- Type
- protein
- Length
- 111 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE
- UniProt
- D1A230
- Ligands
- NI
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE | protein | 111 | 23% helix, 42% strand | D1A230 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5C4P · Crystal structure of ArsI C-As lyase solved by Ni-SAD phasing · 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 5C4P · PDBe 5C4P · UniProt D1A230
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