Structure of PDB 1pzg Chain B Binding Site BS02

Receptor Information
>1pzg Chain B (length=328) Species: 508771 (Toxoplasma gondii ME49) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PALVQRRKKVAMIGSGMIGGTMGYLCALRELADVVLYDVVKGMPEGKALD
LSHVTSVVDTNVSVRAEYSYEAALTGADCVIVTAGLTKVPGKPDSEWSRN
DLLPFNSKIIREIGQNIKKYCPKTFIIVVTNPLDCMVKVMCEASGVPTNM
ICGMACMLDSGRFRRYVADALSVSPRDVQATVIGTHGDCMVPLVRYITVN
GYPIQKFIKDGVVTEKQLEEIAEHTKVSGGEIVRFLGQGSAYYAPAASAV
AMATSFLNDEKRVIPCSVYCNGEYGLKDMFIGLPAVIGGAGIERVIELEL
NEEEKKQFQKSVDDVMALNKAVAALQAP
Ligand information
Ligand IDA3D
InChIInChI=1S/C22H28N6O14P2/c1-10(29)11-3-2-4-27(5-11)21-17(32)15(30)12(40-21)6-38-43(34,35)42-44(36,37)39-7-13-16(31)18(33)22(41-13)28-9-26-14-19(23)24-8-25-20(14)28/h2-5,8-9,12-13,15-18,21-22,30-33H,6-7H2,1H3,(H3-,23,24,25,34,35,36,37)/t12-,13-,15-,16-,17-,18-,21-,22-/m1/s1
InChIKeyKPVQNXLUPNWQHM-RBEMOOQDSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.5CC(=O)c1ccc[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O
CACTVS 3.385CC(=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)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.7.5CC(=O)c1ccc[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)([O-])O[P@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O
CACTVS 3.385CC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
FormulaC22 H28 N6 O14 P2
Name3-ACETYLPYRIDINE ADENINE DINUCLEOTIDE
ChEMBL
DrugBankDB03363
ZINC
PDB chain1pzg Chain B Residue 603 [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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PDB1pzg Structure of Toxoplasma gondii LDH1: Active-Site Differences from Human Lactate Dehydrogenases and the Structural Basis for Efficient APAD+ Use.
Resolution1.6 Å
Binding residue
(original residue number in PDB)		G29 M30 I31 D53 V54 T97 A98 G99 L100 T101 I119 V138 T139 N140 L142 M163 H195 P250
Binding residue
(residue number reindexed from 1)		G16 M17 I18 D38 V39 T83 A84 G85 L86 T87 I109 V129 T130 N131 L133 M154 H186 P245
Annotation score4
Binding affinityMOAD: Ki=25mM
Enzymatic activity
Catalytic site (original residue number in PDB) R109 D168 R171 H195
Catalytic site (residue number reindexed from 1) R99 D159 R162 H186
Enzyme Commision number 1.1.1.27: L-lactate dehydrogenase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004459 L-lactate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Biological Process
GO:0006089 lactate metabolic process
GO:0006090 pyruvate metabolic process
GO:0019752 carboxylic acid metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1pzg, PDBe:1pzg, PDBj:1pzg
PDBsum1pzg
PubMed14744130
UniProtP90613

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