MolNFT v1 · #167171 · protein

Crystal structure of E.COLI rpph in complex with GTP

6VCQ · RNA pyrophosphohydrolase: “Crystal structure of E.COLI rpph in complex with GTP”. X-ray diffraction, 2 ligands (GTP, SO4), 1 pocket (best druggability 0.31). MolNFT v1 #167171 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 6VCQ
Type: protein
Length: 158 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: GTP, SO4
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA pyrophosphohydrolase (EC 3.6.1.-)	protein	158	30% helix, 31% strand	P0A776

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · chains A
SO4 · Sulfate ion · ion · 5 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	77	0.31	0.74	20	GTP

Compared structures

6VCQ · Crystal structure of E.coli RppH in complex with GTP · 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 6VCQ · PDBe 6VCQ · UniProt P0A776

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