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E. COLI rpph structure, ki soak

Analyse E. COLI rpph structure, ki soak in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4S2V
Type: protein
Length: 139 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: CA, IOD

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA pyrophosphohydrolase (EC 3.6.1.-)	protein	139	30% helix, 33% strand	P0A776

Ligands and binding sites

CA · Calcium ion · metal · chains A
IOD · Iodide ion · ion · 27 copies · chains A
ACT · Acetate ion · additive · chains A

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

Compared structures

4S2V · E. coli RppH structure, KI soak · 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 0.91

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 4S2V · PDBe 4S2V · UniProt P0A776

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