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Structure of E. COLI rpph bound to sulfate ions

Analyse Structure of E. COLI rpph bound to sulfate ions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4S2W
Type: protein
Length: 157 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA pyrophosphohydrolase
EC: 3.6.1.-
UniProt: P0A776
Ligands: SO4
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA pyrophosphohydrolase (EC 3.6.1.-)	protein	157	29% helix, 31% strand	P0A776

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	108	0.34	0.73	24	SO4

Compared structures

4S2W · Structure of E. coli RppH bound to sulfate ions · the same entry in another collection · chain A against A, TM-score 1.00
P0A776 · AlphaFold monomer V2.0 prediction for RNA pyrophosphohydrolase (P0A776) · 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 P0A776
Elsewhere: RCSB PDB 4S2W · PDBe 4S2W · UniProt P0A776

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