MolNFT v1 · #149573 · protein
Full length ectodomain of ectonucleotide PHOSPHODIESTERASE/PYROPHOSPHATASE-3 (NPP3) including the smb domains but with a partially disordered active site structure
6G4G: “Full length ectodomain of ectonucleotide PHOSPHODIESTERASE/PYROPHOSPHATASE-3 (NPP3) including the smb domains…”. X-ray diffraction, 2 ligands (NAG, CA). MolNFT v1 #149573 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6G4G
- Type
- protein
- Length
- 3,047 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P97675
- Ligands
- NAG, CA
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 765 | — | P97675 |
| B | — | protein | 759 | — | P97675 |
| C | — | protein | 742 | — | P97675 |
| D | — | protein | 781 | — | P97675 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 22 copies · chains A, B, C, D
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6G4G · Full length ectodomain of ectonucleotide phosphodiesterase/pyrophosphatase-3 (NPP3)… · the same entry in another collection · chain D against D, TM-score 1.00
- P97675 · AlphaFold monomer V2.0 prediction for ectonucleotide PYROPHOSPHATASE/PHOSPHODIESTERASE… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P97675
- Elsewhere: RCSB PDB 6G4G · PDBe 6G4G · UniProt P97675
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