MolNFT v1 · #52744 · protein
The active site of a carbohydrate esterase displays divergent catalytic and non-catalytic binding functions
2W9X: “The active site of a carbohydrate esterase displays divergent catalytic and non-catalytic binding functions”. X-ray diffraction. MolNFT v1 #52744 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2W9X
- Type
- protein
- Length
- 641 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B3PDE5
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 312 | — | B3PDE5 |
| B | — | protein | 329 | — | B3PDE5 |
Compared structures
- 2W9X · The active site of a carbohydrate esterase displays divergent catalytic and non-catalytic… · the same entry in another collection · chain A against A, TM-score 1.00
- B3PDE5 · AlphaFold monomer V2.0 prediction for acetylxylan esterase / glucomannan deacetylase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 B3PDE5
- Elsewhere: RCSB PDB 2W9X · PDBe 2W9X · UniProt B3PDE5
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