Structure of PDB 6cty Chain E

Receptor sequence

>6ctyE (length=341) Species: 632 (Yersinia pestis)

PQTLKIRRPDDWHIHLRDDEMLSTVLPYTSEVFARAIVMPNLAQPITTVA
SAIAYRERILAAVPAGHKFTPLMTCYLTNSLDAKELTTGFEQGVFTAAKL
YPANNSTHGVSDIPAIYPLFEQMQKIGMPLLIHGEVTDAAVDIFDREARF
IDQILEPIRQKFPELKIVFEHITTKDAADYVLAGNRFLGATVTPQHLMFN
RNHMLVGGIRPHLFCLPILKRSTHQQALRAAVASGSDRFFLGTDSAPHAK
HRKESSCGCAGVFNAPAALPAYASVFEELNALQHLEAFCALNGPRFYGLP
VNDDVVELVRTPFLQPEEIPLGNESVIPFLAGQTLNWSVKR

3D structure

• PDB: 6cty Pyrimidine biosynthesis in pathogens - Structures and analysis of dihydroorotases from Yersinia pestis and Vibrio cholerae.
• Chain: E
• Resolution: 2.41 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H17 H19 K103 H140 H178 D251
• Catalytic site (residue number reindexed from 1): H13 H15 K99 H133 H171 D244
• 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	E	H17 H19 K103 D251	H13 H15 K99 D244
BS02	ZN	E	K103 H140 H178	K99 H133 H171

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:0019856 pyrimidine nucleobase biosynthetic process
• GO:0044205 'de novo' UMP biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:6cty, PDBe:6cty, PDBj:6cty
• PDBsum: 6cty
• PubMed: 31207330
• UniProt: Q8ZFU4|PYRC_YERPE Dihydroorotase (Gene Name=pyrC)