Research workbench
Crystal structure of human P32, a doughnut-shaped acidic mitochondrial matrix protein
Analyse Crystal structure of human P32, a doughnut-shaped acidic mitochondrial matrix… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P32
- Type
- protein
- Length
- 529 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial matrix protein, SF2P32
- UniProt
- Q07021
- Pockets
- 8 · best druggability 0.56
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitochondrial matrix protein, SF2P32 | protein | 182 | 36% helix, 26% strand | Q07021 |
| B | Mitochondrial matrix protein, SF2P32 | protein | 171 | 40% helix, 28% strand | Q07021 |
| C | Mitochondrial matrix protein, SF2P32 | protein | 176 | 39% helix, 27% strand | Q07021 |
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 | 173 | 0.56 | 0.81 | 31 | empty |
| 2 | 104 | 0.47 | 0.80 | 18 | empty |
| 3 | 194 | 0.45 | 0.74 | 26 | empty |
| 4 | 156 | 0.43 | 0.74 | 23 | empty |
| 5 | 122 | 0.37 | 0.73 | 22 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1282 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 1254 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 1241 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 1P32 · Crystal structure of human P32, a doughnut-shaped acidic mitochondrial matrix protein · the same entry in another collection · chain A against A, TM-score 1.00
- Q07021 · AlphaFold monomer V2.0 prediction for complement component 1 Q subcomponent-binding… · a predicted model of the same protein · chain C against A, TM-score 0.98
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 Q07021
- Elsewhere: RCSB PDB 1P32 · PDBe 1P32 · UniProt Q07021
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