Research workbench
D202K mutant of P. denitrificans ATP12P
Analyse D202K mutant of P. denitrificans ATP12P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZD2
- Type
- protein
- Length
- 468 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP12 ATPase
- UniProt
- A1B060
- Pockets
- 8 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ATP12 ATPase | protein | 234 | 60% helix, 9% strand | A1B060 |
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 310 | 0.52 | 0.74 | 38 | empty |
| 2 | 167 | 0.43 | 0.74 | 24 | empty |
| 3 | 74 | 0.35 | 0.76 | 16 | empty |
| 4 | 63 | 0.32 | 0.76 | 17 | empty |
| 5 | 81 | 0.31 | 0.73 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 236 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2ZD2 · D202K mutant of P. denitrificans Atp12p · 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 A1B060
- Elsewhere: RCSB PDB 2ZD2 · PDBe 2ZD2 · UniProt A1B060
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