Structure of PDB 4bjh Chain A

Receptor sequence

>4bjhA (length=422) Species: 63363 (Aquifex aeolicus)

MLKLIVKNGYVIDPSQNLEGEFDILVENGKIKKIDKNILVPEAEIIDAKG
LIVCPGFIDIHVHLRDPGQTYKEDIESGSRCAVAGGFTTIVCMPNTNPPI
DNTTVVNYILQKSKSVGLCRVLPTGTITKGRKGKEIADFYSLKEAGCVAF
TDDGSPVMDSSVMRKALELASQLGVPIMDACEDDKLAYGVINEGEVSALL
GLSSRAPEAEEIQIARDGILAQRTGGHVHIQAVSTKLSLEIIEFFKEKGV
KITCEVNPNHLLFTEREVLNSGANARVNPPLRKKEDRLALIEGVKRGIID
CFATDHAPHQTFEKELVEFAMPGIIGLQTALPSALELYRKGIISLKKLIE
MFTINPARIIGVDLGTLKLGSPADITIFDPNKEWILNEETNLSKSRNTPL
WGKVLKGKVIYTIKDGKMVYKD

3D structure

• PDB: 4bjh The Mononuclear Metal Center of Type-I Dihydroorotase from Aquifex Aeolicus.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H61 H63
• Catalytic site (residue number reindexed from 1): H61 H63
• 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 D305	H61 H63 D153 D305
BS02	DOR	A	H63 R65 G154 V277 N278 H309 P322 G323	H63 R65 G154 V277 N278 H309 P322 G323

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:4bjh, PDBe:4bjh, PDBj:4bjh
• PDBsum: 4bjh
• PubMed: 24314009
• UniProt: O66990|PYRC_AQUAE Dihydroorotase (Gene Name=pyrC)