Research workbench
Structure of the nuclease subunit of human mitochondrial RNase P (MRPP3) at 1.98A
Analyse Structure of the nuclease subunit of human mitochondrial RNase P (MRPP3) at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XGM
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial ribonuclease P protein 3
- EC
- 3.1.26.5
- UniProt
- O15091
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitochondrial ribonuclease P protein 3 (EC 3.1.26.5) | protein | 341 | 47% helix, 14% strand | O15091 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 214 | 0.60 | 0.81 | 34 | empty |
| 2 | 51 | 0.37 | 0.80 | 11 | empty |
| 3 | 51 | 0.32 | 0.77 | 15 | empty |
| 4 | 52 | 0.26 | 0.73 | 13 | GOL |
Compared structures
- 4XGM · Structure of the nuclease subunit of human mitochondrial RNase P (MRPP3) at 1.98A · the same entry in another collection · chain A against A, TM-score 1.00
- O15091 · AlphaFold monomer V2.0 prediction for mitochondrial ribonuclease P catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 O15091
- Elsewhere: RCSB PDB 4XGM · PDBe 4XGM · UniProt O15091
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