Research workbench
Solution structure of the family 1 carbohydrate-binding module with mannosylated THR1
Analyse Solution structure of the family 1 carbohydrate-binding module with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5X35
- Type
- protein
- Length
- 36 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exoglucanase 1
- EC
- 3.2.1.91
- UniProt
- P62694
- Ligands
- MAN
Structure
solution nmr · 1 distinct chain · 0% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exoglucanase 1 (EC 3.2.1.91) | protein | 36 | 0% helix, 25% strand | P62694 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide, 1 glycan (disulfide, O-glycosylation).
Compared structures
- 5X35 · Solution structure of the Family 1 carbohydrate-binding module with mannosylated Thr1 · the same entry in another collection · chain A against A, TM-score 1.00
- P62694 · AlphaFold monomer V2.0 prediction for exoglucanase 1 (P62694) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P62694
- Elsewhere: RCSB PDB 5X35 · PDBe 5X35 · UniProt P62694
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