Research workbench
Structure of lpmo in complex with cellotetraose at 3.6X10^5 gy
Analyse Structure of lpmo in complex with cellotetraose at 3.6X10^5 gy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PYG
- 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, NAG, CU, CL
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Auxiliary activity 9 | protein | 235 | 9% helix, 30% strand | A0A0S2GKZ1 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 4 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
- CU · Copper (II) ion · metal · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide, 1 glycan, 1 modified (disulfide, N-glycosylation, methylation).
Compared structures
- 7PYG · Structure of LPMO in complex with cellotetraose at 3.6x10^5 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 7PYG · PDBe 7PYG · UniProt A0A0S2GKZ1
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