Research workbench
Structural basis for the acyl chain selectivity and mechanism of udp- N-acetylglucosamine acyltransferase
Analyse Structural basis for the acyl chain selectivity and mechanism of udp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QIV
- Type
- protein
- Length
- 262 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylglucosamine acyltransferase
- EC
- 2.3.1.129
- UniProt
- P0A722
- Ligands
- U21
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Udp-N-acetylglucosamine acyltransferase (EC 2.3.1.129) | protein | 262 | 17% helix, 30% strand | P0A722 |
Ligands and binding sites
- U21 · uridine-5'-diphosphate-3-O-(R-3-hydroxydecanoyl)-N-acetyl-D-glucosamine · ligand · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2QIV · Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine… · the same entry in another collection · chain X against X, TM-score 1.00
- P0A722 · AlphaFold monomer V2.0 prediction for acyl-[acyl-carrier… · a predicted model of the same protein · chain X against A, TM-score 1.00
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 P0A722
- Elsewhere: RCSB PDB 2QIV · PDBe 2QIV · UniProt P0A722
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