MolNFT v1 · #128849 · protein
Extended catalytic domain of H. jecorina LPMO9A A.K.A EG4
5O2X · Glycoside hydrolase family 61: “Extended catalytic domain of H. jecorina LPMO9A A.K.A EG4”. X-ray diffraction, 4 ligands (MAN, NAG, CU). MolNFT v1 #128849 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5O2X
- Type
- protein
- Length
- 248 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycoside hydrolase family 61
- UniProt
- G0R6T8
- Ligands
- MAN, NAG, CU, SO4
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycoside hydrolase family 61 | protein | 248 | 9% helix, 33% strand | G0R6T8 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 15 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- CU · Copper (II) 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: 17 glycan, 2 disulfide, 1 modified (O-glycosylation, disulfide, N-glycosylation, methylation).
Compared structures
- 5O2X · Extended catalytic domain of H. jecorina LPMO9A a.k.a EG4 · 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 G0R6T8
- Elsewhere: RCSB PDB 5O2X · PDBe 5O2X · UniProt G0R6T8
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