Structure of PDB 1xrf Chain A

Receptor sequence

>1xrfA (length=363) Species: 63363 (Aquifex aeolicus)

WMLKLIVKNGYVIDPSQNLEGEFDILVENGKIKKIDKNILVPEAEIIDAK
GLIVCPGFIDIHVHLRDPGQTYKEDIESGSRCAVAGGFTTIVCMPNTNPP
IDNTTVVNYILQKSKSVGLCRVLPTGTITKGRKGKEIADFYSLKEAGCVA
FTDDGSPVMDSSVMRKALELASQLGVPIMDHAEEIQIARDGILAQRTGGH
VHIQHVSTKLSLEIIEFFKEKGVKITCEVNPNHLLDRLALIEGVKRGIID
CFATDHAPHQTMPGIIGLQTALPSALELYRKGIISLKKLIEMFTINPARI
IGVDLGTLKLGSPADITIFDPNKEWILNEETNLSKSRNTPLWGKVLKGKV
IYTIKDGKMVYKD

3D structure

• PDB: 1xrf The crystal structure of a novel, latent dihydroorotase from Aquifex aeolicus at 1.7A resolution
• Chain: A
• Resolution: 1.65 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H61 H63
• Catalytic site (residue number reindexed from 1): H62 H64
• 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	H61 H63 D153	H62 H64 D154

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:1xrf, PDBe:1xrf, PDBj:1xrf
• PDBsum: 1xrf
• PubMed: 15826652
• UniProt: O66990|PYRC_AQUAE Dihydroorotase (Gene Name=pyrC)