Structure of PDB 1b8u Chain A Binding Site BS02

Receptor Information
>1b8u Chain A (length=327) Species: 87645 (Aquaspirillum arcticum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KTPMRVAVTGAAGQICYSLLFRIANGDMLGKDQPVILQLLEIPNEKAQKA
LQGVMMEIDDCAFPLLAGMTAHADPMTAFKDADVALLVGARPRGPGMERK
DLLEANAQIFTVQGKAIDAVASRNIKVLVVGNPANTNAYIAMKSAPSLPA
KNFTAMLRLDHNRALSQIAAKTGKPVSSIEKLFVWGNHSPTMYADYRYAQ
IDGASVKDMINDDAWNRDTFLPTVGKRGAAIIDARGVSSAASAANAAIDH
IHDWVLGTAGKWTTMGIPSDGSYGIPEGVIFGFPVTTENGEYKIVQGLSI
DAFSQERINVTLNELLEEQNGVQHLLG
Ligand information
Ligand IDNAD
InChIInChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
SMILES
SoftwareSMILES
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)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)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)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]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)O)O)O)O)C(=O)N
FormulaC21 H27 N7 O14 P2
NameNICOTINAMIDE-ADENINE-DINUCLEOTIDE
ChEMBLCHEMBL1234613
DrugBankDB14128
ZINC
PDB chain1b8u Chain A Residue 334 [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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PDB1b8u Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		T11 G12 G15 Q16 I17 E43 I44 V90 Q115 V132 G133 N134 M158 H190
Binding residue
(residue number reindexed from 1)		T9 G10 G13 Q14 I15 E41 I42 V88 Q113 V130 G131 N132 M156 H188
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D162 H190
Catalytic site (residue number reindexed from 1) D160 H188
Enzyme Commision number 1.1.1.37: malate dehydrogenase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016491 oxidoreductase activity
GO:0016615 malate dehydrogenase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0030060 L-malate dehydrogenase (NAD+) activity
Biological Process
GO:0006099 tricarboxylic acid cycle
GO:0006107 oxaloacetate metabolic process
GO:0006108 malate metabolic process
GO:0006734 NADH metabolic process
GO:0019752 carboxylic acid metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1b8u, PDBe:1b8u, PDBj:1b8u
PDBsum1b8u
PubMed10206992
UniProtQ9ZF99|MDH_AQUAR Malate dehydrogenase (Gene Name=mdh)

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