Research workbench
CBM29-2 mutant D114A: probing the mechanism of ligand recognition by family 29 carbohydrate binding modules
Analyse CBM29-2 mutant D114A: probing the mechanism of ligand recognition by family 29… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W90
- Type
- protein
- Length
- 293 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-catalytic protein 1
- UniProt
- Q9C171
- Ligands
- NA
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Non-catalytic protein 1 | protein | 151 | 5% helix, 51% strand | Q9C171 |
| B | Non-catalytic protein 1 | protein | 142 | 0% helix, 54% strand | Q9C171 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1W90 · CBM29-2 mutant D114A: Probing the Mechanism of Ligand Recognition by Family 29… · 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 Q9C171
- Elsewhere: RCSB PDB 1W90 · PDBe 1W90 · UniProt Q9C171
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