Structure of PDB 6hfr Chain A

Receptor sequence
>6hfrA (length=362) Species: 9606 (Homo sapiens) [Search protein sequence]
KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPP
IIDGPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYL
NETYSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRS
VHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGE
VRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSRPPPGFPGLET
MLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWT
IPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDV
RKWPQGAVPQLP
3D structure
PDB6hfr Characterization of the catalytic flexible loop in the dihydroorotase domain of the human multi-enzymatic protein CAD.
ChainA
Resolution1.29949 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
BS04 NCD A H1473 R1475 K1556 T1562 Y1563 H1590 H1614 V1660 R1661 D1686 A1688 H1690 P1702 G1703 H14 R16 K97 T103 Y104 H131 H155 V201 R202 D227 A229 H231 P243 G244
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:6hfr, PDBe:6hfr, PDBj:6hfr
PDBsum6hfr
PubMed30315107
UniProtP27708|PYR1_HUMAN Multifunctional protein CAD (Gene Name=CAD)

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