MolNFT v1 · #13124 · protein
The crystal structure and catalytic mechanism of cellobiohydrolase cels, the major enzymatic component of the clostridium thermocellum cellulosome
1L1Y: “The crystal structure and catalytic mechanism of cellobiohydrolase cels, the major enzymatic component of the…”. X-ray diffraction. MolNFT v1 #13124 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1L1Y
- Type
- protein
- Length
- 3,852 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P38686
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 642 | — | P38686 |
Compared structures
- 1L1Y · The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major… · the same entry in another collection · 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 P38686
- Elsewhere: RCSB PDB 1L1Y · PDBe 1L1Y · UniProt P38686
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