Research workbench
Structure of uncomplexed carbohydrate binding domain CBM36
Analyse Structure of uncomplexed carbohydrate binding domain CBM36 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W0N
- Type
- protein
- Length
- 120 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-beta-xylanase D
- EC
- 3.2.1.8
- UniProt
- P45796
- Ligands
- CA, MG, SO4
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 63% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase D (EC 3.2.1.8) | protein | 120 | 3% helix, 63% strand | P45796 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1W0N · Structure of uncomplexed Carbohydrate Binding Domain CBM36 · the same entry in another collection · chain A against A, TM-score 1.00
- P45796 · AlphaFold monomer V2.0 prediction for arabinoxylan arabinofuranohydrolase (P45796) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P45796
- Elsewhere: RCSB PDB 1W0N · PDBe 1W0N · UniProt P45796
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