Research workbench
Catalytic domain of endo-1,4-glucanase CEL6A from thermobifida fusca in complex with methyl cellobiosyl-4-thio-beta-cellobioside
Analyse Catalytic domain of endo-1,4-glucanase CEL6A from thermobifida fusca in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BOD
- Type
- protein
- Length
- 279 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P26222
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | — | protein | 279 | — | P26222 |
Compared structures
- 2BOD · Catalytic domain of endo-1,4-glucanase Cel6A from Thermobifida fusca in complex with… · the same entry in another collection · chain X against X, TM-score 1.00
- P26222 · AlphaFold monomer V2.0 prediction for endoglucanase E-2 (P26222) · a predicted model of the same protein · chain X 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 P26222
- Elsewhere: RCSB PDB 2BOD · PDBe 2BOD · UniProt P26222
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.