Structure of PDB 5g1p Chain E

Receptor sequence

>5g1pE (length=299) Species: 9606 (Homo sapiens)

HSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASM
FYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYA
DVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELG
TVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSMPPTVRAFVA
SRGTKQEEFESIEEALPDTDVLYMTRIQKERFGYEACFGQFILTPHIMTR
AKKKMVVMHPMPRVNEISVESDPRAAYFRQAENGMYIRMALLATVLGRF

3D structure

• PDB: 5g1p Structure and Functional Characterization of Human Aspartate Transcarbamoylase, the Target of the Anti-Tumoral Drug Pala.
• Chain: E
• Resolution: 3.19 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R1975 T1976 K2003 R2024 H2052 Q2055 T2145 P2184 G2210
• Catalytic site (residue number reindexed from 1): R57 T58 K85 R106 H134 Q137 T225 P260 G284
• 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	CP	E	S1973 R1975 T1976 R2024 Q2055 M2185	S55 R57 T58 R106 Q137 M261	PDBbind-CN: -logKd/Ki=5.20,Kd=6.3uM

Gene Ontology

Molecular Function

• GO:0004070 aspartate carbamoyltransferase activity
• GO:0016597 amino acid binding
• GO:0016743 carboxyl- or carbamoyltransferase activity

Biological Process

• GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
• GO:0006520 amino acid metabolic process

External links

• PDB: RCSB:5g1p, PDBe:5g1p, PDBj:5g1p
• PDBsum: 5g1p
• PubMed: 27265852
• UniProt: P27708|PYR1_HUMAN Multifunctional protein CAD (Gene Name=CAD)