Structure of PDB 6hfd Chain A

Receptor sequence
>6hfdA (length=362) Species: 9606 (Homo sapiens) [Search protein sequence]
KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPP
IIDGPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYL
NETLSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRS
VHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGE
VRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSRPPPGFPGLET
MLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWT
IPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDV
RKWPQGAVPQLP
3D structure
PDB6hfd Characterization of the catalytic flexible loop in the dihydroorotase domain of the human multi-enzymatic protein CAD.
ChainA
Resolution1.86997 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 H131 H155
BS02 ZN A H1471 H1473 K1556 D1686 H12 H14 K97 D227
BS03 ZN A H1471 C1613 E1637 H12 C154 E178
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:6hfd, PDBe:6hfd, PDBj:6hfd
PDBsum6hfd
PubMed30315107
UniProtP27708|PYR1_HUMAN Multifunctional protein CAD (Gene Name=CAD)

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