Structure of PDB 1pqu Chain A Binding Site BS01

Receptor Information
>1pqu Chain A (length=371) Species: 71421 (Haemophilus influenzae Rd KW20) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKNVGFIGWRGMVGSVLMDRMSQENDFENLNPVFFTTSQAGQKAPVFGGK
DAGDLKSAFDIEELKKLDIIVTCQGGDYTNEVYPKLKATGWDGYWVDAAS
ALRMKDDAIIVLDPVNQHVISEGLKKGIKTFVGGNCTVSLMLMAIGGLFE
KDLVEWISVATYQAASGAGAKNMRELLSQMGLLEQAVSSELKDPASSILD
IERKVTAKMRADNFPTDNFGAALGGSLIPWIDKLLPETGQTKEEWKGYAE
TNKILGLSDNPIPVDGLCVRIGALRCNSQAFTIKLKKDLPLEEIEQIIAS
HNEWVKVIPNDKEITLRELTPAKVTGTLSVPVGRLRKLAMGPEYLAAFTV
GDQLLWGAAEPVRRILKQLVA
Ligand information
Ligand IDNAP
InChIInChI=1S/C21H28N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1-4,7-8,10-11,13-16,20-21,29-31H,5-6H2,(H7-,22,23,24,25,32,33,34,35,36,37,38,39)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyXJLXINKUBYWONI-NNYOXOHSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N
FormulaC21 H28 N7 O17 P3
NameNADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;
2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
ChEMBLCHEMBL295069
DrugBankDB03461
ZINC
PDB chain1pqu Chain A Residue 1372 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1pqu The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.
Resolution1.92 Å
Binding residue
(original residue number in PDB)		G8 R10 G11 M12 V13 T36 T37 S38 C73 Q74 A99 S166 L354 A358
Binding residue
(residue number reindexed from 1)		G8 R10 G11 M12 V13 T36 T37 S38 C73 Q74 A99 S166 L354 A358
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) C136 Q163 R270 N277
Catalytic site (residue number reindexed from 1) C136 Q163 R270 N277
Enzyme Commision number 1.2.1.11: aspartate-semialdehyde dehydrogenase.
Gene Ontology
Molecular Function
GO:0004073 aspartate-semialdehyde dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0046983 protein dimerization activity
GO:0050661 NADP binding
GO:0051287 NAD binding
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009085 lysine biosynthetic process
GO:0009086 methionine biosynthetic process
GO:0009088 threonine biosynthetic process
GO:0009089 lysine biosynthetic process via diaminopimelate
GO:0009097 isoleucine biosynthetic process
GO:0019877 diaminopimelate biosynthetic process
GO:0071266 'de novo' L-methionine biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1pqu, PDBe:1pqu, PDBj:1pqu
PDBsum1pqu
PubMed15272161
UniProtP44801|DHAS_HAEIN Aspartate-semialdehyde dehydrogenase (Gene Name=asd)

[Back to BioLiP]