Research workbench
Copper binding protein from laetisaria arvalis (LAX325)
Analyse Copper binding protein from laetisaria arvalis (LAX325) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IBH
- Type
- protein
- Length
- 299 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Auxiliary activity cazyme
- Ligands
- NAG, CU
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Auxiliary activity cazyme | protein | 150 | 13% helix, 39% strand | — |
| B | Auxiliary activity cazyme | protein | 149 | 13% helix, 40% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 11 copies · chains A, B
- CU · Copper (II) ion · metal · 2 copies · chains A, B
- IMD · Imidazole · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 325 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 glycan, 4 disulfide (N-glycosylation, disulfide).
Compared structures
- 6IBH · Copper binding protein from Laetisaria arvalis (LaX325) · 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
- Elsewhere: RCSB PDB 6IBH · PDBe 6IBH
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