Research workbench

Apo form of S. cerevisiae orotate phosphoribosyltransferase

Analyse Apo form of S. cerevisiae orotate phosphoribosyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PRY
Type: protein
Length: 215 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Orotate phosphoribosyltransferase 1
EC: 2.4.2.10
UniProt: P13298
Ligands: MG
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Orotate phosphoribosyltransferase 1 (EC 2.4.2.10)	protein	215	41% helix, 24% strand	P13298

Ligands and binding sites

MG · Magnesium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	199	0.51	0.76	29	empty
2	91	0.45	0.80	23	empty
3	51	0.32	0.77	11	empty

Compared structures

2PRY · Apo form of S. cerevisiae orotate phosphoribosyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
P13298 · AlphaFold monomer V2.0 prediction for orotate phosphoribosyltransferase 1 (P13298) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P13298
Elsewhere: RCSB PDB 2PRY · PDBe 2PRY · UniProt P13298

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