Research workbench
AA9 lytic polysaccharide monooxygenase (lpmo) from malbranchea cinnamomea
Analyse AA9 lytic polysaccharide monooxygenase (lpmo) from malbranchea cinnamomea in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NTL
- Type
- protein
- Length
- 219 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LPMO9F
- UniProt
- A0A5J6BJN2
- Ligands
- SNN, CU
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | LPMO9F | protein | 219 | 9% helix, 33% strand | A0A5J6BJN2 |
Ligands and binding sites
- SNN · L-3-aminosuccinimide · ligand · chains A
- CU · Copper (II) ion · metal · chains A
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 covalent, 2 disulfide (covalent ligand, disulfide).
Compared structures
- 7NTL · AA9 lytic polysaccharide monooxygenase (LPMO) from Malbranchea cinnamomea · 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 A0A5J6BJN2
- Elsewhere: RCSB PDB 7NTL · PDBe 7NTL · UniProt A0A5J6BJN2
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