MolNFT v1 · #16084 · protein
The first crystallographic structure of a xylanase from glycosyl hydrolase family 5: implications for catalysis
1NOF: “The first crystallographic structure of a xylanase from glycosyl hydrolase family 5: implications for…”. X-ray diffraction. MolNFT v1 #16084 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1NOF
- Type
- protein
- Length
- 383 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Xylanase
- EC
- 3.2.1.8
- UniProt
- Q46961
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xylanase (EC 3.2.1.8) | protein | 383 | 27% helix, 32% strand | Q46961 |
Ligands and binding sites
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1NOF · The first crystallographic structure of a xylanase from glycosyl hydrolase family 5… · 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 Q46961
- Elsewhere: RCSB PDB 1NOF · PDBe 1NOF · UniProt Q46961
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.