Structure of PDB 8pbr Chain A

Receptor sequence
>8pbrA (length=361) Species: 9606 (Homo sapiens) [Search protein sequence]
AKLVRLPGLIDVHVHLQEPTHKEDFASGTAAALAGGITMVCAMPNTRPPI
IDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYLN
ETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSV
HICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEV
RPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSRPPPGFPGLETM
LPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTI
PSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVR
KWPQGAVPQLP
3D structure
PDB8pbr Beyond genetics: Deciphering the impact of missense variants in CAD deficiency.
ChainA
Resolution2.06 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 H1471 H1473 K1556 D1686 H13 H15 K96 D226
BS02 ZN A K1556 H1590 H1614 K96 H130 H154
BS03 ZN A E1524 G1804 G1806 E64 G344 G346
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:8pbr, PDBe:8pbr, PDBj:8pbr
PDBsum8pbr
PubMed37540500
UniProtP27708|PYR1_HUMAN Multifunctional protein CAD (Gene Name=CAD)

[Back to BioLiP]