Research workbench
Catalytic domain of the major endoglucanase from xanthomonas campestris pv. campestris
Analyse Catalytic domain of the major endoglucanase from xanthomonas campestris pv.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4TUF
- Type
- protein
- Length
- 1,384 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P19487
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 346 | — | P19487 |
Compared structures
- 4TUF · Catalytic domain of the major endoglucanase from Xanthomonas campestris pv. campestris · the same entry in another collection · chain A against A, TM-score 1.00
- P19487 · AlphaFold monomer V2.0 prediction for major extracellular endoglucanase (P19487) · 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 P19487
- Elsewhere: RCSB PDB 4TUF · PDBe 4TUF · UniProt P19487
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