Research workbench
Structure of ligand-bound mouse cgamp hydrolase ENPP1
Analyse Structure of ligand-bound mouse cgamp hydrolase ENPP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XKD
- Type
- protein
- Length
- 1,360 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- G3X9S2
- Ligands
- IJE, NAG, BMA, MAN, ZN, CA, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 679 | — | G3X9S2 |
| B | — | protein | 681 | — | G3X9S2 |
Ligands and binding sites
- IJE · {2-[1-(6,7-dimethoxyquinazolin-4-yl)piperidin-4-yl]ethyl}phosphonic acid · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 2 copies
- MAN · alpha-D-mannopyranose · sugar · 2 copies
- ZN · Zinc ion · metal · 4 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6XKD · Structure of ligand-bound mouse cGAMP hydrolase ENPP1 · 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 G3X9S2
- Elsewhere: RCSB PDB 6XKD · PDBe 6XKD · UniProt G3X9S2
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