Structure of PDB 4bjh Chain B

Receptor sequence
>4bjhB (length=291) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
MRSLISSLDLTREEVEEILKYAKEFKEGKEETIKASAVLFFSEPSTRTRL
SFEKAARELGIETYLVSGSESSTVKGESFFDTLKTFEGLGFDYVVFRVPF
VFFPYKEIVKSLNLRLVNAGDGTHQHPSQGLIDFFTIKEHFGEVKDLRVL
YVGDIKHSRVFRSGAPLLNMFGAKIGVCGPKTLIPRDVEVFKVDVFDDVD
KGIDWADVVIWLRLQKERQKENYIPSESSYFKQFGLTKERFEKVKLYMHP
GPVNRNVDIDHELVYTEKSLIQEQVKNGIPVRKAIYKFLWT
3D structure
PDB4bjh The Mononuclear Metal Center of Type-I Dihydroorotase from Aquifex Aeolicus.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R47 T48 K75 R97 H126 Q129
Catalytic site (residue number reindexed from 1) R47 T48 K75 R97 H126 Q129
Enzyme Commision number 2.1.3.2: aspartate carbamoyltransferase.
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 PAL B S45 T46 R47 T48 R97 H126 R159 V160 R213 Q215 G251 S45 T46 R47 T48 R97 H126 R159 V160 R213 Q215 G251
Gene Ontology
Molecular Function
GO:0004070 aspartate carbamoyltransferase activity
GO:0016597 amino acid binding
GO:0016740 transferase activity
GO:0016743 carboxyl- or carbamoyltransferase activity
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0006520 amino acid metabolic process
GO:0044205 'de novo' UMP biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4bjh, PDBe:4bjh, PDBj:4bjh
PDBsum4bjh
PubMed24314009
UniProtO66726|PYRB_AQUAE Aspartate carbamoyltransferase catalytic subunit (Gene Name=pyrB)

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