Structure of PDB 4yiw Chain A

Receptor sequence

>4yiwA (length=424) Species: 1392 (Bacillus anthracis)

NYLFKNGRYMNEEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLI
APGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCR
EHMEDLQNRIKEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDD
GVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHGL
NGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKV
TAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHEALIEGLLDGTIDMI
ATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQ
FLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPF
AGWKCQGWPVMTIVGGKIAWQKES

3D structure

• PDB: 4yiw Ca-asp bound X-ray structure and inhibition of Bacillus anthracis dihydroorotase (DHOase).
• Chain: A
• Resolution: 2.45 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H59 H61
• Catalytic site (residue number reindexed from 1): H58 H60
• 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	H58 H60 D150 D303
BS02	ZN	A	D151 H178 H231	D150 H177 H230
BS03	NCD	A	R63 M276 N277 D304 F322 G323	R62 M275 N276 D303 F321 G322

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:4yiw, PDBe:4yiw, PDBj:4yiw
• PDBsum: 4yiw
• PubMed: 27499369
• UniProt: Q81WF0|PYRC_BACAN Dihydroorotase (Gene Name=pyrC)