Structure of PDB 5g1n Chain E Binding Site BS02

Receptor Information
>5g1n Chain E (length=307) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASM
FYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYA
DVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELG
TVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAF
VASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFGQFILT
PHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALL
ATVLGRF
Ligand information
Ligand IDPAL
InChIInChI=1S/C6H10NO8P/c8-4(2-16(13,14)15)7-3(6(11)12)1-5(9)10/h3H,1-2H2,(H,7,8)(H,9,10)(H,11,12)(H2,13,14,15)/t3-/m0/s1
InChIKeyZZKNRXZVGOYGJT-VKHMYHEASA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC(=O)C[CH](NC(=O)C[P](O)(O)=O)C(O)=O
CACTVS 3.341OC(=O)C[C@H](NC(=O)C[P](O)(O)=O)C(O)=O
ACDLabs 10.04O=C(NC(C(=O)O)CC(=O)O)CP(=O)(O)O
OpenEye OEToolkits 1.5.0C(C(C(=O)O)NC(=O)CP(=O)(O)O)C(=O)O
OpenEye OEToolkits 1.5.0C([C@@H](C(=O)O)NC(=O)CP(=O)(O)O)C(=O)O
FormulaC6 H10 N O8 P
NameN-(PHOSPHONACETYL)-L-ASPARTIC ACID
ChEMBLCHEMBL504802
DrugBankDB03459
ZINCZINC000001563934
PDB chain5g1n Chain E Residue 3226 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5g1n Structure and Functional Characterization of Human Aspartate Transcarbamoylase, the Target of the Anti-Tumoral Drug Pala.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		S1973 T1974 R1975 T1976 R2024 H2052 R2085 R2146 Q2148 M2185
Binding residue
(residue number reindexed from 1)		S55 T56 R57 T58 R106 H134 R167 R228 Q230 M267
Annotation score1
Binding affinityMOAD: Kd=0.017uM
PDBbind-CN: -logKd/Ki=7.77,Kd=0.017uM
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 T227 P266 G292
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).
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5g1n, PDBe:5g1n, PDBj:5g1n
PDBsum5g1n
PubMed27265852
UniProtP27708|PYR1_HUMAN Multifunctional protein CAD (Gene Name=CAD)

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