Research workbench
Human ectonucleoside triphosphate diphosphohydrolase 4 (ENTPD4, ntpdase 4)
Analyse Human ectonucleoside triphosphate diphosphohydrolase 4 (ENTPD4, ntpdase 4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WG5
- Type
- protein
- Length
- 492 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ectonucleoside triphosphate diphosphohydrolase 4
- EC
- 3.6.1.6
- UniProt
- Q9Y227
- Ligands
- NAG
- Pockets
- 6 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ectonucleoside triphosphate diphosphohydrolase 4 (EC 3.6.1.6) | protein | 492 | 40% helix, 21% strand | Q9Y227 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 352 | 0.58 | 0.76 | 35 | empty |
| 2 | 86 | 0.57 | 0.87 | 21 | empty |
| 3 | 182 | 0.53 | 0.79 | 27 | empty |
| 4 | 115 | 0.43 | 0.77 | 21 | empty |
| 5 | 97 | 0.43 | 0.79 | 17 | empty |
Modifications
Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 6WG5 · Human ectonucleoside triphosphate diphosphohydrolase 4 (ENTPD4, NTPDase 4) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y227 · AlphaFold monomer V2.0 prediction for ectonucleoside triphosphate diphosphohydrolase 4… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q9Y227
- Elsewhere: RCSB PDB 6WG5 · PDBe 6WG5 · UniProt Q9Y227
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