Research workbench
Crystal structure of apo pino from porphyromonas gingivitis
Analyse Crystal structure of apo pino from porphyromonas gingivitis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R2H
- Type
- protein
- Length
- 375 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hmuy protein
- UniProt
- A0A1P8JNE7
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hmuy protein | protein | 191 | 7% helix, 48% strand | A0A1P8JNE7 |
| B | Hmuy protein | protein | 184 | 8% helix, 51% strand | A0A1P8JNE7 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 626 | 0.66 | 0.76 | 47 | empty |
| 2 | 475 | 0.66 | 0.78 | 49 | empty |
Interfaces
1 interface between chains.
- A–B · 656 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6R2H · Crystal structure of Apo PinO from Porphyromonas gingivitis · 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 A0A1P8JNE7
- Elsewhere: RCSB PDB 6R2H · PDBe 6R2H · UniProt A0A1P8JNE7
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