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Crystal structure of methanothermobacter thermautotrophicus orotidine 5'-monophosphate decarboxylase complexed with pyrazofurin monophosphate

Analyse Crystal structure of methanothermobacter thermautotrophicus orotidine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3SEC
Type: protein
Length: 214 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: PFU
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23)	protein	214	51% helix, 19% strand	O26232

Ligands and binding sites

PFU · (1S)-1,4-anhydro-1-(5-carbamoyl-4-hydroxy-1H-pyrazol-3-yl)-5-O-phosphono-D-ribitol · ligand · chains A
GOL · Glycerol · additive · 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	159	0.56	0.81	29	PFU
2	55	0.34	0.77	13	empty

Compared structures

3SEC · Crystal structure of Methanothermobacter thermautotrophicus orotidine 5'-monophosphate… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt O26232
Elsewhere: RCSB PDB 3SEC · PDBe 3SEC · UniProt O26232

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