Structure of PDB 3mpg Chain A

Receptor sequence

>3mpgA (length=426) Species: 1392 (Bacillus anthracis)

MNYLFKNGRYMNEEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKL
IAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDC
REHMEDLQNRIKEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTD
DGVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHG
LNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIK
VTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHEALIEGLLDGTIDM
IATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTNLVKKGIITLEQLI
QFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTP
FAGWKCQGWPVMTIVGGKIAWQKESA

3D structure

• PDB: 3mpg Structure of dihydroorotase from Bacillus anthracis at 2.6A resolution.
• Chain: A
• Resolution: 2.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H59 H61
• Catalytic site (residue number reindexed from 1): H59 H61
• 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	H59 H61 D151 D304	H59 H61 D151 D304
BS02	ZN	A	D151 H178 H231	D151 H178 H231

Gene Ontology

Molecular Function

• GO:0004038 allantoinase activity
• GO:0004151 dihydroorotase activity
• GO:0008270 zinc ion binding
• GO:0016787 hydrolase activity
• GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
• GO:0016812 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
• GO:0046872 metal ion binding

Biological Process

• GO:0006145 purine nucleobase catabolic process
• GO:0006221 pyrimidine nucleotide biosynthetic process
• GO:0044205 'de novo' UMP biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:3mpg, PDBe:3mpg, PDBj:3mpg
• PDBsum: 3mpg
• PubMed: 21045288
• UniProt: Q81WF0|PYRC_BACAN Dihydroorotase (Gene Name=pyrC)