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Wild-type orotidine 5'-monophosphate decarboxylase from M. thermoautotrophicus complexed with 6-methyl-ump

Analyse Wild-type orotidine 5'-monophosphate decarboxylase from M. thermoautotrophicus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WJW
Type: protein
Length: 215 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: O26232
Ligands: U6M
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23)	protein	215	52% helix, 19% strand	O26232

Ligands and binding sites

U6M · 6-methyluridine 5'-(dihydrogen phosphate) · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	138	0.55	0.82	29	U6M

Compared structures

3WJW · Wild-type orotidine 5'-monophosphate decarboxylase from M. thermoautotrophicus complexed… · 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 O26232
Elsewhere: RCSB PDB 3WJW · PDBe 3WJW · UniProt O26232

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