MolNFT v2 · #155132 · protein
Catalytic domain of GH87 alpha-1,3-glucanase D1068A in complex with nigerose
6K0Q: “Catalytic domain of GH87 alpha-1,3-glucanase D1068A in complex with nigerose”. X-ray diffraction at 1.564, 4 ligands (GLC, BGC, CA). MolNFT v2 #155132 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6K0Q
- Type
- protein
- Length
- 559 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.564
- Source
- Paenibacillus glycanilyticus
- UniProt
- A0A068PS59
- Ligands
- GLC, BGC, CA, SO4
Structure
x-ray diffraction · resolution 1.564 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 559 | — | A0A068PS59 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 5 copies · chains A
- BGC · beta-D-glucopyranose · sugar · chains A
- CA · Calcium ion · metal · chains A
- SO4 · Sulfate ion · ion · 5 copies · chains A
- ACY · Acetic acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6K0Q · Catalytic domain of GH87 alpha-1,3-glucanase D1068A in complex with nigerose · 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 A0A068PS59
- Elsewhere: RCSB PDB 6K0Q · PDBe 6K0Q · UniProt A0A068PS59
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