MolNFT v1 · #185513 · protein
Structure of lpmo (expressed in E.COLI) with cellotriose at 5.62X10^4 gy
7PYW · Auxiliary activity 9: “Structure of lpmo (expressed in E.COLI) with cellotriose at 5.62X10^4 gy”. X-ray diffraction, 4 ligands (BGC, CU, SO4). MolNFT v1 #185513 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7PYW
- Type
- protein
- Length
- 235 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Auxiliary activity 9
- UniProt
- A0A0S2GKZ1
- Ligands
- BGC, CU, SO4, CL
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Auxiliary activity 9 | protein | 235 | 8% helix, 30% strand | A0A0S2GKZ1 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 5 copies · chains A
- CU · Copper (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7PYW · Structure of LPMO (expressed in E.coli) with cellotriose at 5.62x10^4 Gy · 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 A0A0S2GKZ1
- Elsewhere: RCSB PDB 7PYW · PDBe 7PYW · UniProt A0A0S2GKZ1
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