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PAB0955 crystal structure : a GTPase in GDP and mg bound form from pyrococcus abyssi (after GTP hydrolysis)

Analyse PAB0955 crystal structure : a GTPase in GDP and mg bound form from pyrococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OXR
Type: protein
Length: 246 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP(GTP)BINDING protein
UniProt: Q9UYR9
Ligands: GDP, MG
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATP(GTP)BINDING protein	protein	246	50% helix, 13% strand	Q9UYR9

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · 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	220	0.56	0.78	28	empty
2	62	0.32	0.76	20	MG

Compared structures

2OXR · PAB0955 crystal structure : a GTPase in GDP and Mg bound form from Pyrococcus abyssi… · the same entry in another collection · chain A against A, TM-score 1.00
Q9UYR9 · AlphaFold monomer V2.0 prediction for gpn-loop GTPase PAB0955 (Q9UYR9) · 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 Q9UYR9
Elsewhere: RCSB PDB 2OXR · PDBe 2OXR · UniProt Q9UYR9

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