Structure of PDB 5m66 Chain A Binding Site BS04

Receptor Information
>5m66 Chain A (length=468) Species: 29448 (Bradyrhizobium elkanii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GFTDYIVKDIALADFGRKEISLAETEMPGLMATREEYGPKQPLKGARIAG
SLHMTIQTAVLIETLAALGADIRWVSCNIYSTQDHAAAAIAAAGIPVFAV
KGETLTEYWDYTAKLFDWHGGGTPNMILDDGGDATMLVHAGYRAEQGDTA
FLDKPGSEEEEIFYALVKRLLKEKPKGWFAEIAKNIKGVSEETTTGVHRL
YEMANKGTLLFPAINVNDSVTKSKFDNLYGCRESLVDGIRRGTDVMLSGK
VAMVAGFGDVGKGSAASLRQAGCRVMVSEVDPICALQAAMEGYEVVTMED
AAPRADIFVTATGNKDIITIEHMRAMKDRAIVCNIGHFDNEIQIASLRNL
KWTNIKPQVDEIEFPDKHRIIMLSEGRLVNLGNAMGHPSFVMSASFTNQT
LAQIELFANNKDSKYAKKVYVLPKTLDEKVARLHLAKIGVKLTELRKDQA
DYIGVKQEGPYKSDHYRY
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 chain5m66 Chain B Residue 501 [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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PDB5m66 Crystallographic and SAXS studies of S-adenosyl-l-homocysteine hydrolase from Bradyrhizobium elkanii.
Resolution1.951 Å
Binding residue
(original residue number in PDB)		K467 Y471
Binding residue
(residue number reindexed from 1)		K462 Y466
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) H58 S81 S86 D135 E197 N222 K227 D231 N232 C236 H342 H392 S400 Q404
Catalytic site (residue number reindexed from 1) H53 S76 S81 D130 E192 N217 K222 D226 N227 C231 H337 H387 S395 Q399
Enzyme Commision number 3.13.2.1: adenosylhomocysteinase.
Gene Ontology
Molecular Function
GO:0004013 adenosylhomocysteinase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006730 one-carbon metabolic process
GO:0033353 S-adenosylmethionine cycle
GO:0071269 L-homocysteine biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5m66, PDBe:5m66, PDBj:5m66
PDBsum5m66
PubMed28512574
UniProtA0A087WNH6|SAHH_BRAEL Adenosylhomocysteinase (Gene Name=ahcY)

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