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Structure of nucleotide triphosphate pyrophosphatase from pyrococcus horikoshii OT3

Analyse Structure of nucleotide triphosphate pyrophosphatase from pyrococcus horikoshii… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1V7R
Type: protein
Length: 186 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein PH1917
EC: 3.6.1.19
UniProt: O59580
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein PH1917 (EC 3.6.1.19)	protein	186	39% helix, 26% strand	O59580

Ligands and binding sites

CIT · Citric acid · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.51	0.85	18	empty
2	115	0.46	0.79	23	empty

Compared structures

1V7R · Structure of nucleotide triphosphate pyrophosphatase from pyrococcus horikoshii OT3 · the same entry in another collection · chain A against A, TM-score 1.00
O59580 · AlphaFold monomer V2.0 prediction for DITP/XTP pyrophosphatase (O59580) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O59580
Elsewhere: RCSB PDB 1V7R · PDBe 1V7R · UniProt O59580

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