Research workbench
Hydrogen bonding and catalysis: an unexpected explanation for how a single amino acid substitution can change the pH optimum of a glycosidase
Analyse Hydrogen bonding and catalysis: an unexpected explanation for how a single… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C5H
- Type
- protein
- Length
- 185 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P09850
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 185 | — | P09850 |
Compared structures
- 1C5H · Hydrogen bonding and catalysis: an unexpected explanation for how a single amino acid… · the same entry in another collection · chain A against A, TM-score 1.00
- P09850 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P09850) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P09850
- Elsewhere: RCSB PDB 1C5H · PDBe 1C5H · UniProt P09850
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