Structure of PDB 4lfy Chain A

Receptor sequence

>4lfyA (length=349) Species: 216591 (Burkholderia cenocepacia J2315)

PPMTASNSPATLSLARPDDWHLHLRDGDMLAAVLPHTARQFGRAIVMPNL
KPPVTTTAQAQAYRERILAALPAGMTFEPLMTLYLTDNTPPDEIRRARES
GFVHGVKLYPASDHGVTDLAKCAKTLEAMQETGMPLLVHGEVTDASIDLF
DREKVFIDRVMTPLRRDFPGLKVVFEHITTKDAADYVRDADAAPGLLGAT
ITAHHLLYNRNALFVGGIRPHYYCLPVLKRETHRVALVEAATSGNPRFFL
GTDSAPHARDAKETACGCAGCYTALHALELYAEAFDTAGALDKLEGFASF
FGADFYGLPRSAETVTLRREPWELPREIFAGETPVVPLRGGETIGWKLA

3D structure

• PDB: 4lfy Crystal structure of a dihydroorotase from Burkholderia cenocepacia J2315
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H31 H33 K117 H154 H192 D268
• Catalytic site (residue number reindexed from 1): H21 H23 K107 H139 H177 D253
• Enzyme Commision number: 3.5.2.3: dihydroorotase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	A	H31 H33 K117 D268	H21 H23 K107 D253
BS02	ZN	A	K117 H154 H192	K107 H139 H177
BS03	CA	A	R245 E246 T247	R230 E231 T232
BS04	CA	A	R225 R245	R210 R230

Gene Ontology

Molecular Function

• GO:0004151 dihydroorotase activity
• GO:0008270 zinc ion binding
• GO:0016787 hydrolase activity
• GO:0016812 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
• GO:0046872 metal ion binding

Biological Process

• GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
• GO:0006221 pyrimidine nucleotide biosynthetic process
• GO:0009220 pyrimidine ribonucleotide biosynthetic process
• GO:0019856 pyrimidine nucleobase biosynthetic process
• GO:0044205 'de novo' UMP biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:4lfy, PDBe:4lfy, PDBj:4lfy
• PDBsum: 4lfy
• UniProt: B4EEU0