Research workbench
C-terminal xylan binding domain from cellulomonas fimi xylanase 11A
Analyse C-terminal xylan binding domain from cellulomonas fimi xylanase 11A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HEH
- Type
- protein
- Length
- 88 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-beta-xylanase D
- EC
- 3.2.1.8
- UniProt
- P54865
Structure
solution nmr · 1 distinct chain · 0% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Endo-1,4-beta-xylanase D (EC 3.2.1.8) | protein | 88 | 0% helix, 32% strand | P54865 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1HEH · C-terminal xylan binding domain from Cellulomonas fimi xylanase 11A · the same entry in another collection · chain C against C, TM-score 1.00
- P54865 · AlphaFold monomer V2.0 prediction for bifunctional XYLANASE/DEACETYLASE (P54865) · a predicted model of the same protein · chain C against A, TM-score 0.83
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 P54865
- Elsewhere: RCSB PDB 1HEH · PDBe 1HEH · UniProt P54865
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