Structure of PDB 4c6e Chain A

Receptor sequence

>4c6eA (length=364) Species: 9606 (Homo sapiens)

KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPP
IIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYL
NETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRS
VHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGE
VRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSRPPPGFPGLET
MLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWT
IPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDV
RKWPQGAVPQLPPS

3D structure

• PDB: 4c6e Structure, Functional Characterization and Evolution of the Dihydroorotase Domain of Human Cad.
• Chain: A
• Resolution: 1.263 Å

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	DOR	A	H1473 R1475 T1562 F1563 H1590 V1660 R1661 A1688 H1690 P1702 G1703	H14 R16 T103 F104 H131 V201 R202 A229 H231 P243 G244
BS02	NCD	A	H1473 R1475 K1556 T1562 F1563 H1590 V1660 R1661 D1686 A1688 H1690 P1702 G1703	H14 R16 K97 T103 F104 H131 V201 R202 D227 A229 H231 P243 G244
BS03	ZN	A	H1471 H1473 K1556 D1686	H12 H14 K97 D227
BS04	ZN	A	K1556 H1590 H1614	K97 H131 H155

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

External links

• PDB: RCSB:4c6e, PDBe:4c6e, PDBj:4c6e
• PDBsum: 4c6e
• PubMed: 24332717
• UniProt: P27708|PYR1_HUMAN Multifunctional protein CAD (Gene Name=CAD)