Research workbench

RNase P protein from staphylococcus aureus

Analyse RNase P protein from staphylococcus aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1D6T
Type: protein
Length: 117 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease P
EC: 3.1.26.5
UniProt: P0A0H5
Pockets: 1 · best druggability 0.35

Structure

solution nmr · 1 distinct chain · 38% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonuclease P (EC 3.1.26.5)	protein	117	38% helix, 14% strand	P0A0H5

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	73	0.35	0.76	13	empty

Compared structures

1D6T · RNase P protein from staphylococcus aureus · 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 0.85

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 1D6T · PDBe 1D6T · UniProt P0A0H5

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