MolNFT v1 · #119187 · protein
Crystal structure of the catalytic domain of NCLPMO9A
5FOH · Polysaccharide monooxygenase: “Crystal structure of the catalytic domain of NCLPMO9A”. X-ray diffraction, 4 ligands (MAN, CU, LI). MolNFT v1 #119187 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5FOH
- Type
- protein
- Length
- 218 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polysaccharide monooxygenase
- UniProt
- Q7S439
- Ligands
- MAN, CU, LI, SO4
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polysaccharide monooxygenase | protein | 218 | 6% helix, 35% strand | Q7S439 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
- CU · Copper (II) ion · metal · chains A
- LI · Lithium ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide, 2 glycan (disulfide, O-glycosylation).
Compared structures
- 5FOH · Crystal structure of the catalytic domain of NcLPMO9A · 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 Q7S439
- Elsewhere: RCSB PDB 5FOH · PDBe 5FOH · UniProt Q7S439
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