Research workbench
Crystal structure of bifunctional protein fold from helicobacter pylori
Analyse Crystal structure of bifunctional protein fold from helicobacter pylori in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6APE
- Type
- protein
- Length
- 284 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional protein fold
- EC
- 1.5.1.5, 3.5.4.9
- UniProt
- B5Z6U8
- Ligands
- NA
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional protein fold (EC 1.5.1.5, 3.5.4.9) | protein | 284 | 45% helix, 17% strand | B5Z6U8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 483 | 0.69 | 0.79 | 46 | GOL |
| 2 | 53 | 0.29 | 0.74 | 12 | empty |
| 3 | 63 | 0.28 | 0.72 | 11 | empty |
Compared structures
- 6APE · Crystal Structure of Bifunctional protein FolD from Helicobacter pylori · 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 B5Z6U8
- Elsewhere: RCSB PDB 6APE · PDBe 6APE · UniProt B5Z6U8
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