Research workbench
Crystal structure of an archaeal chitinase in the ligand-free form
Analyse Crystal structure of an archaeal chitinase in the ligand-free form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XSV
- Type
- protein
- Length
- 1,942 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A161KIT4
- Ligands
- CO, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 486 | — | A0A161KIT4 |
| B, C | — | protein | 485 | — | A0A161KIT4 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · 14 copies · chains A, C, B, D
- SO4 · Sulfate ion · ion · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5XSV · Crystal structure of an archaeal chitinase in the ligand-free 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 A0A161KIT4
- Elsewhere: RCSB PDB 5XSV · PDBe 5XSV · UniProt A0A161KIT4
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