Research workbench
Cellulomonas fimi XYLANASE/CELLULASE double mutant E127A/H205N with covalent cellobiose
Analyse Cellulomonas fimi XYLANASE/CELLULASE double mutant E127A/H205N with covalent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HIS
- Type
- protein
- Length
- 312 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P07986
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 312 | — | P07986 |
Compared structures
- 2HIS · Cellulomonas fimi XYLANASE/CELLULASE double mutant E127A/H205N with covalent cellobiose · the same entry in another collection · chain A against A, TM-score 1.00
- P07986 · AlphaFold monomer V2.0 prediction for EXOGLUCANASE/XYLANASE (P07986) · a predicted model of the same protein · 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 P07986
- Elsewhere: RCSB PDB 2HIS · PDBe 2HIS · UniProt P07986
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