Research workbench
Crystal structure of carbon-nitrogen hydrolase from helicobacter pylori G27
Analyse Crystal structure of carbon-nitrogen hydrolase from helicobacter pylori G27 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MG6
- Type
- protein
- Length
- 1,172 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbon-nitrogen hydrolase
- UniProt
- B5Z7B9
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbon-nitrogen hydrolase | protein | 294 | 35% helix, 28% strand | B5Z7B9 |
| B, C | Carbon-nitrogen hydrolase | protein | 293 | 35% helix, 28% strand | B5Z7B9 |
| D | Carbon-nitrogen hydrolase | protein | 292 | 36% helix, 28% strand | B5Z7B9 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 270 | 0.75 | 0.89 | 43 | empty |
| 2 | 408 | 0.69 | 0.81 | 55 | empty |
| 3 | 331 | 0.67 | 0.81 | 33 | empty |
| 4 | 206 | 0.64 | 0.83 | 28 | empty |
| 5 | 313 | 0.63 | 0.79 | 29 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2783 Ų buried · 50 hydrogen bonds · protein-protein
- C–D · 2412 Ų buried · 43 hydrogen bonds · protein-protein
- B–C · 741 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 535 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 490 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6MG6 · Crystal structure of carbon-nitrogen hydrolase from Helicobacter pylori G27 · 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 B5Z7B9
- Elsewhere: RCSB PDB 6MG6 · PDBe 6MG6 · UniProt B5Z7B9
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