Research workbench
2.45 ångström resolution crystal structure of udp-N-acetylglucosamine 1-carboxyvinyltransferase from campylobacter jejuni.
Analyse 2.45 ångström resolution crystal structure of udp-N-acetylglucosamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UJS
- Type
- protein
- Length
- 848 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9PP65
- Ligands
- CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 417 | — | Q9PP65 |
| B | — | protein | 431 | — | Q9PP65 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5UJS · 2.45 Angstrom Resolution Crystal Structure of UDP-N-acetylglucosamine… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9PP65 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9PP65
- Elsewhere: RCSB PDB 5UJS · PDBe 5UJS · UniProt Q9PP65
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