Structure of PDB 3gri Chain A

Receptor sequence

>3griA (length=422) Species: 196620 (Staphylococcus aureus subsp. aureus MW2)

MKLIKNGKVLQNGELQQADILIDGKVIKQIAPAIEPSNGVDIIDAKGHFV
SPGFVDVHVHLREPGGEYKETIETGTKAAARGGFTTVCPMPNTRPVPDSV
EHFEALQKLIDDNAQVRVLPYASITTRQLGKELVDFPALVKEGAFAFTDD
GVGVQTASMMYEGMIEAAKVNKAIVAHCEDNSLIYGGAMHEGKRSKELGI
PGIPNICESVQIARDVLLAEAAGCHYHVCHVSTKESVRVIRDAKRAGIHV
TAEVTPHHLLLTEDDIPGNNAIYKMNPPLRSTEDREALLEGLLDGTIDCI
ATDHAPHARDEKAQPMEKAPFGIVGSETAFPLLYTHFVKNGDWTLQQLVD
YLTIKPCETFNLEYGTLKENGYADLTIIDLDSEQEIKGEDFLSKADNTPF
IGYKVYGNPILTMVEGEVKFEG

3D structure

• PDB: 3gri The Crystal Structure of a Dihydroorotase from Staphylococcus aureus
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• 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	H58 H60 D303	H58 H60 D303
BS02	CA	A	F391 L392 S393	F391 L392 S393

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:3gri, PDBe:3gri, PDBj:3gri
• PDBsum: 3gri
• UniProt: P65907|PYRC_STAAW Dihydroorotase (Gene Name=pyrC)