Research workbench
Nucleotide substrate binding by udp-N-acetylglucosamine acyltransferase
Analyse Nucleotide substrate binding by udp-N-acetylglucosamine acyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JF3
- Type
- protein
- Length
- 262 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl-[acyl-carrier-protein]--udp-N- acetylglucosamine O-acyltransferase
- EC
- 2.3.1.129
- UniProt
- P0A722
- Ligands
- UD1
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyl-[acyl-carrier-protein]--udp-N- acetylglucosamine O-acyltransferase (EC 2.3.1.129) | protein | 262 | 18% helix, 29% strand | P0A722 |
Ligands and binding sites
- UD1 · Uridine-diphosphate-N-acetylglucosamine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 2JF3 · PDBe 2JF3 · UniProt P0A722
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