Structure of PDB 5g1p Chain B

Receptor sequence
>5g1pB (length=288) Species: 9606 (Homo sapiens) [Search protein sequence]
SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMF
YEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYAD
VVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGT
VNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFV
ASRGTKQEEFESIEEALPDTDVLYMTRFILTPHIMTRAKKKMVVMHPMPR
VNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF
3D structure
PDB5g1p Structure and Functional Characterization of Human Aspartate Transcarbamoylase, the Target of the Anti-Tumoral Drug Pala.
ChainB
Resolution3.19 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) R56 T57 K84 R105 H133 Q136 T226 P247 G273
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 B R1975 T1976 Q2055 R56 T57 Q136
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5g1p, PDBe:5g1p, PDBj:5g1p
PDBsum5g1p
PubMed27265852
UniProtP27708|PYR1_HUMAN Multifunctional protein CAD (Gene Name=CAD)

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