MolNFT v1 · #148969 · protein
Crystal structure of human udp-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1)
6FM9: “Crystal structure of human udp-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase…”. X-ray diffraction, 1 ligand (P6L). MolNFT v1 #148969 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6FM9
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9H3H5
- Ligands
- P6L
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 378 | — | Q9H3H5 |
Ligands and binding sites
- P6L · (2S)-3-{[{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-2-[(6E)-hexadec-6-enoyloxy]propyl (8E)-octadec-8-enoate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FM9 · 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 0.98
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 6FM9 · PDBe 6FM9 · UniProt Q9H3H5
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