Research workbench
Ddahb, GDP-mannoheptose C3,5 epimerase from campylobacter jejuni complexed to GDP-mannose
Analyse Ddahb, GDP-mannoheptose C3,5 epimerase from campylobacter jejuni complexed to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ANJ
- Type
- protein
- Length
- 335 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thymidine diphospho-4-keto-rhamnose 3,5-epimerase
- EC
- 5.1.3.13
- UniProt
- Q6EF58
- Ligands
- GDD, GDP
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thymidine diphospho-4-keto-rhamnose 3,5-epimerase (EC 5.1.3.13) | protein | 172 | 8% helix, 48% strand | Q6EF58 |
| B | Thymidine diphospho-4-keto-rhamnose 3,5-epimerase (EC 5.1.3.13) | protein | 163 | 4% helix, 48% strand | Q6EF58 |
Ligands and binding sites
- GDD · Guanosine-5'-diphosphate-alpha-D-mannose · ligand · chains A, B
- GDP · Guanosine-5'-diphosphate · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 272 | 0.53 | 0.75 | 35 | empty |
| 2 | 148 | 0.45 | 0.76 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 1825 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 7ANJ · DdahB, GDP-mannoheptose C3,5 epimerase from Campylobacter jejuni complexed to GDP-mannose · 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 Q6EF58
- Elsewhere: RCSB PDB 7ANJ · PDBe 7ANJ · UniProt Q6EF58
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