MolNFT v1 · #119255 · protein
The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from clostridium perfringens
5FQG: “The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase…”. X-ray diffraction. MolNFT v1 #119255 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5FQG
- Type
- protein
- Length
- 583 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0H2YNR7
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 583 | — | A0A0H2YNR7 |
Compared structures
- 5FQG · The details of glycolipid glycan hydrolysis by the structural analysis of a family 123… · 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 A0A0H2YNR7
- Elsewhere: RCSB PDB 5FQG · PDBe 5FQG · UniProt A0A0H2YNR7
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