Research workbench
X-ray crystal structure of GDP-D-glycero-D-manno-heptose 4,6- dehydratase from campylobacter jejuni
Analyse X-ray crystal structure of GDP-D-glycero-D-manno-heptose 4,6- dehydratase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7US5
- Type
- protein
- Length
- 1,373 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5M6Q7
- Ligands
- NAD, GDP
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 346 | — | Q5M6Q7 |
| B, C | — | protein | 342 | — | Q5M6Q7 |
| D | — | protein | 343 | — | Q5M6Q7 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, B, C, D
- GDP · Guanosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7US5 · X-ray crystal structure of GDP-D-glycero-D-manno-heptose 4,6-Dehydratase from… · the same entry in another collection · chain A 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 Q5M6Q7
- Elsewhere: RCSB PDB 7US5 · PDBe 7US5 · UniProt Q5M6Q7
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