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Crystal structure of the polysaccharide deacetylase BC1974 from bacillus cereus in complex with (2S)-2-amino-5- (diaminomethylideneamino)-N-hydroxypentanamide
Analyse Crystal structure of the polysaccharide deacetylase BC1974 from bacillus cereus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NCD
- Type
- protein
- Length
- 824 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0A3VTA3
- Ligands
- AHL, ZN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 206 | — | A0A0A3VTA3 |
Ligands and binding sites
- AHL · N-hydroxy-L-argininamide · ligand · chains B
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
- ACT · Acetate ion · additive · 3 copies · chains A, D, B, C
- CIT · Citric acid · additive · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NCD · Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in… · 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 A0A0A3VTA3
- Elsewhere: RCSB PDB 5NCD · PDBe 5NCD · UniProt A0A0A3VTA3
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