Structure of PDB 1pzf Chain A Binding Site BS02

Receptor Information

>1pzf Chain A (length=328) Species: 5811 (Toxoplasma gondii)

PALVQRRKKVAMIGSGMIGGTMGYLCALRELADVVLYDVVKGMPEGKALD
LSHVTSVVDTNVSVRAEYSYEAALTGADCVIVTAGLTKVPGKPDSEWSRN
DLLPFNSKIIREIGQNIKKYCPKTFIIVVTNPLDCMVKVMCEASGVPTNM
ICGMACMLDSGRFRRYVADALSVSPRDVQATVIGTHGDCMVPLVRYITVN
GYPIQKFIKDGVVTEKQLEEIAEHTKVSGGEIVRFLGQGSAYYAPAASAV
AMATSFLNDEKRVIPCSVYCNGEYGLKDMFIGLPAVIGGAGIERVIELEL
NEEEKKQFQKSVDDVMALNKAVAALQAP

Ligand information

• Ligand ID: A3D
• InChI: InChI=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
• InChIKey: KPVQNXLUPNWQHM-RBEMOOQDSA-N
• SMILES:
  OpenEye OEToolkits 1.7.5: CC(=O)c1ccc[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O
  CACTVS 3.385: CC(=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 1.7.5: CC(=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 3.385: CC(=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
• Formula: C22 H28 N6 O14 P2
• Name: 3-ACETYLPYRIDINE ADENINE DINUCLEOTIDE
• DrugBank: DB03363
• PDB chain: 1pzf Chain A Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1pzf Structure of Toxoplasma gondii LDH1: Active-Site Differences from Human Lactate Dehydrogenases and the Structural Basis for Efficient APAD+ Use.
• Resolution: 2.2 Å
• Binding residue (original residue number in PDB): G29 M30 I31 D53 V54 T97 A98 G99 L100 T101 I119 V138 N140 L142 M163 L167 H195 P250
• Binding residue (residue number reindexed from 1): G16 M17 I18 D38 V39 T83 A84 G85 L86 T87 I109 V129 N131 L133 M154 L158 H186 P245
• Annotation score: 4

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

External links

• PDB: RCSB:1pzf, PDBe:1pzf, PDBj:1pzf
• PDBsum: 1pzf
• PubMed: 14744130
• UniProt: P90613