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Crystal structure of orotidine 5'-phosphate decarboxylase (TM0332) from thermotoga maritima at 2.00 a resolution

Analyse Crystal structure of orotidine 5'-phosphate decarboxylase (TM0332) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VQT
Type: protein
Length: 191 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Orotidine 5'-phosphate decarboxylase
EC: 4.1.1.23
UniProt: Q9WYG7
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23)	protein	191	42% helix, 21% strand	Q9WYG7

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 9 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	163	0.49	0.77	26	EDO

Compared structures

1VQT · Crystal structure of Orotidine 5'-phosphate decarboxylase (TM0332) from Thermotoga… · the same entry in another collection · chain A against A, TM-score 1.00
Q9WYG7 · AlphaFold monomer V2.0 prediction for orotidine 5'-phosphate decarboxylase (Q9WYG7) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9WYG7
Elsewhere: RCSB PDB 1VQT · PDBe 1VQT · UniProt Q9WYG7

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