MolNFT v2 · #125999 · protein
Crystal structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) (V264G mutant)
5LEV: “Crystal structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase…”. X-ray diffraction at 3.2, 1 ligand (UNL). MolNFT v2 #125999 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5LEV
- Type
- protein
- Length
- 375 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.2
- Source
- Homo sapiens
- UniProt
- Q9H3H5
- Ligands
- UNL
Structure
x-ray diffraction · resolution 3.2 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 375 | — | Q9H3H5 |
Ligands and binding sites
- UNL · Unknown ligand · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5LEV · Crystal structure of human udp-N-acetylglucosamine-dolichyl-phosphate… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H3H5 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine-- dolichyl-phosphate… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9H3H5
- Elsewhere: RCSB PDB 5LEV · PDBe 5LEV · UniProt Q9H3H5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.