Structure of PDB 1ep2 Chain A

Receptor sequence

>1ep2A (length=305) Species: 1358 (Lactococcus lactis)

ENNRLSVKLPGLDLKNPIIPASGCFGFGEEYAKYYDLNKLGSIMVKATTL
HPRFGNPTPRVAETASGMLNAIGLQNPGLEVIMTEKLPWLNENFPELPII
ANVAGSEEADYVAVCAKIGDAANVKAIELNISCPNGQAFGTDPEVAAALV
KACKAVSKVPLYVKLSPNVTDIVPIAKAVEAAGADGLTMINTLMGVRFDL
KTRQPILANITGGLSGPAIKPVALKLIHQVAQDVDIPIIGMGGVANAQDV
LEMYMAGASAVAVGTANFADPFVCPKIIDKLPELMDQYRIESLESLIQEV
KEGKK

3D structure

• PDB: 1ep2 Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster.
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K48 N72 L76 C135 N137 K170 N197
• Catalytic site (residue number reindexed from 1): K46 N70 L74 C133 N135 K164 N191
• Enzyme Commision number: 1.3.1.14: dihydroorotate dehydrogenase (NAD(+)).

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	FMN	A	S24 G25 C26 K48 A49 N72 N104 N132 K170 N197 S221 G222 M247 G248 G249 G270 T271	S22 G23 C24 K46 A47 N70 N102 N130 K164 N191 S215 G216 M241 G242 G243 G264 T265

Gene Ontology

Molecular Function

• GO:0004152 dihydroorotate dehydrogenase activity
• GO:0004589 dihydroorotate dehydrogenase (NAD+) activity
• GO:0005515 protein binding
• GO:0016491 oxidoreductase activity
• GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors

Biological Process

• GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
• GO:0006221 pyrimidine nucleotide biosynthetic process
• GO:0006222 UMP biosynthetic process
• GO:0044205 'de novo' UMP biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1ep2, PDBe:1ep2, PDBj:1ep2
• PDBsum: 1ep2
• PubMed: 11188687
• UniProt: P54322|PYRDB_LACLM Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit (Gene Name=pyrDB)