Structure of PDB 6cty Chain D

Receptor sequence
>6ctyD (length=343) Species: 632 (Yersinia pestis) [Search protein sequence]
PQTLKIRRPDDWHIHLRDDEMLSTVLPYTSEVFARAIVMPNLAQPITTVA
SAIAYRERILAAVPAGHKFTPLMTCYLTNSLDAKELTTGFEQGVFTAAKL
YPANATTNSTHGVSDIPAIYPLFEQMQKIGMPLLIHGEVTDAAVDIFDRE
ARFIDQILEPIRQKFPELKIVFEHITTKDAADYVLAGNRFLGATVTPQHL
MFNRNHMLVGGIRPHLFCLPILKRSTHQQALRAAVASGSDRFFLGTDSAP
HAKHRKESSCGCAGVFNAPAALPAYASVFEELNALQHLEAFCALNGPRFY
GLPVNDDVVELVRTPFLQPEEIPLGNESVIPFLAGQTLNWSVK
3D structure
PDB6cty Pyrimidine biosynthesis in pathogens - Structures and analysis of dihydroorotases from Yersinia pestis and Vibrio cholerae.
ChainD
Resolution2.41 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 H136 H174 D247
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 D H17 H19 K103 D251 H13 H15 K99 D247
BS02 ZN D K103 H140 H178 K99 H136 H174
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6cty, PDBe:6cty, PDBj:6cty
PDBsum6cty
PubMed31207330
UniProtQ8ZFU4|PYRC_YERPE Dihydroorotase (Gene Name=pyrC)

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