Research workbench
Structure of staphylococcus aureus RNase P protein at 2.0 ångström
Analyse Structure of staphylococcus aureus RNase P protein at 2.0 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6D1R
- Type
- protein
- Length
- 109 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease P protein component
- EC
- 3.1.26.5
- UniProt
- P0A0H5
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease P protein component (EC 3.1.26.5) | protein | 109 | 45% helix, 22% strand | P0A0H5 |
Compared structures
- 6D1R · Structure of Staphylococcus aureus RNase P protein at 2.0 angstrom · the same entry in another collection · chain A against A, TM-score 1.00
- P0A0H5 · AlphaFold monomer V2.0 prediction for ribonuclease P protein component (P0A0H5) · a predicted model of the same protein · chain A 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 P0A0H5
- Elsewhere: RCSB PDB 6D1R · PDBe 6D1R · UniProt P0A0H5
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