Research workbench
Crystal structure of human udp-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) (V264G mutant)
Analyse Crystal structure of human udp-N-acetylglucosamine-dolichyl-phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LEV
- Type
- protein
- Length
- 375 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9H3H5
- Ligands
- UNL
Structure
x-ray diffraction · 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
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