Structure of PDB 6hg2 Chain A

Receptor sequence
>6hg2A (length=356) Species: 9606 (Homo sapiens) [Search protein sequence]
KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPP
IIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYL
AGVTSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHV
ARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELG
SRQDVEALWENMAVIDCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLL
TAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMP
FSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQG
AVPQLP
3D structure
PDB6hg2 Characterization of the catalytic flexible loop in the dihydroorotase domain of the human multi-enzymatic protein CAD.
ChainA
Resolution1.83 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.3.2: aspartate carbamoyltransferase.
3.5.1.2: glutaminase.
3.5.2.3: dihydroorotase.
6.3.4.16: carbamoyl-phosphate synthase (ammonia).
6.3.5.5: carbamoyl-phosphate synthase (glutamine-hydrolyzing).
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 K1556 H1590 H1614 K97 H125 H149
BS02 ZN A H1471 H1473 K1556 D1686 H12 H14 K97 D221
BS03 FOT A H1473 R1475 N1505 Y1558 H1590 V1660 R1661 H1690 P1702 G1703 H14 R16 N46 Y99 H125 V195 R196 H225 P237 G238
Gene Ontology
Molecular Function
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

View graph for
Molecular Function
External links
PDB RCSB:6hg2, PDBe:6hg2, PDBj:6hg2
PDBsum6hg2
PubMed30315107
UniProtP27708|PYR1_HUMAN Multifunctional protein CAD (Gene Name=CAD)

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