Structure of PDB 2hjr Chain I Binding Site BS01

Receptor Information
>2hjr Chain I (length=313) Species: 5807 (Cryptosporidium parvum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRKKISIIGAGQIGSTIALLLGQKDLGDVYMFDIIEGVPQGKALDLNHCM
ALIGSPAKIFGENNYEYLQNSDVVIITAGVPRKPNMTRSDLLTVNAKIVG
SVAENVGKYCPNAFVICITNPLDAMVYYFKEKSGIPANKVCGMSGVLDSA
RFRCNLSRALGVKPSDVSAIVVGGHGDEMIPLTSSVTIGGILLSDFVEQG
KITHSQINEIIKKTAFGGGEIVELLKTGSAFYAPAASAVAMAQAYLKDSK
SVLVCSTYLTGQYNVNNLFVGVPVVIGKNGIEDVVIVNLSDDEKSLFSKS
VESIQNLVQDLKS
Ligand information
Ligand IDAPR
InChIInChI=1S/C15H23N5O14P2/c16-12-7-13(18-3-17-12)20(4-19-7)14-10(23)8(21)5(32-14)1-30-35(26,27)34-36(28,29)31-2-6-9(22)11(24)15(25)33-6/h3-6,8-11,14-15,21-25H,1-2H2,(H,26,27)(H,28,29)(H2,16,17,18)/t5-,6-,8-,9-,10-,11-,14-,15-/m1/s1
InChIKeySRNWOUGRCWSEMX-KEOHHSTQSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(OCC3OC(n1c2ncnc(N)c2nc1)C(O)C3O)OP(=O)(O)OCC4OC(O)C(O)C4O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)O)O)O)O)O)N
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)O)O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]4O[CH](O)[CH](O)[CH]4O)[CH](O)[CH]3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P@@](O)(=O)OC[C@H]4O[C@@H](O)[C@H](O)[C@@H]4O)[C@@H](O)[C@H]3O
FormulaC15 H23 N5 O14 P2
NameADENOSINE-5-DIPHOSPHORIBOSE
ChEMBLCHEMBL1231026
DrugBank
ZINCZINC000017654550
PDB chain2hjr Chain I Residue 3008 [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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PDB2hjr Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		G23 Q24 I25 D45 I46 I47 Y77 T89 A90 V92 P93 I110 I130 T131 N132
Binding residue
(residue number reindexed from 1)		G11 Q12 I13 D33 I34 I35 Y65 T77 A78 V80 P81 I98 I118 T119 N120
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) R100 D160 R163 H187
Catalytic site (residue number reindexed from 1) R88 D148 R151 H175
Enzyme Commision number 1.1.1.27: L-lactate dehydrogenase.
Gene Ontology
Molecular Function
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:2hjr, PDBe:2hjr, PDBj:2hjr
PDBsum2hjr
PubMed17125854
UniProtQ5CYZ3

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