Structure of PDB 6hg3 Chain A

Receptor sequence
>6hg3A (length=361) Species: 9606 (Homo sapiens) [Search protein sequence]
QKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRP
PIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLY
LASSHGVTSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVH
ICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVR
PELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSRPPPGFPGLETML
PLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIP
SHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRK
WPQGAVPQLPP
3D structure
PDB6hg3 Characterization of the catalytic flexible loop in the dihydroorotase domain of the human multi-enzymatic protein CAD.
ChainA
Resolution1.97 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 H1592 H1616 K98 H129 H153
BS02 ZN A H1471 H1473 K1556 D1688 H13 H15 K98 D225
BS03 DOR A H1473 R1475 Y1558 H1592 V1662 R1663 A1690 H1692 P1704 G1705 H15 R17 Y100 H129 V199 R200 A227 H229 P241 G242
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:6hg3, PDBe:6hg3, PDBj:6hg3
PDBsum6hg3
PubMed30315107
UniProtP27708|PYR1_HUMAN Multifunctional protein CAD (Gene Name=CAD)

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