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Crystal structure of catalytic domain of chitinase from ralstonia sp. a-471 (E162Q)
Analyse Crystal structure of catalytic domain of chitinase from ralstonia sp. a-471… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3W6E
- Type
- protein
- Length
- 613 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B7XCV4
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 158 | — | B7XCV4 |
| B, C | — | protein | 151 | — | B7XCV4 |
| D | — | protein | 153 | — | B7XCV4 |
Compared structures
- 3W6E · Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E162Q) · 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 B7XCV4
- Elsewhere: RCSB PDB 3W6E · PDBe 3W6E · UniProt B7XCV4
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