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Rat NTPDASE2 in complex with mg gmppnp

Analyse Rat NTPDASE2 in complex with mg gmppnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BQZ
Type: protein
Length: 419 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ectonucleoside triphosphate diphosphohydrolase 2
EC: 3.6.1.5
UniProt: Q5RJP4
Ligands: GNP, MG
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ectonucleoside triphosphate diphosphohydrolase 2 (EC 3.6.1.5)	protein	419	40% helix, 24% strand	Q5RJP4

Ligands and binding sites

GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
MG · Magnesium ion · metal · chains A
GOL · Glycerol · additive · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	310	0.65	0.81	44	GNP, MG
2	332	0.54	0.75	38	GOL
3	60	0.33	0.76	16	empty

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

4BQZ · Rat NTPDase2 in complex with Mg GMPPNP · the same entry in another collection · chain A against A, TM-score 1.00

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 Q5RJP4
Elsewhere: RCSB PDB 4BQZ · PDBe 4BQZ · UniProt Q5RJP4

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