Structure of PDB 1ky5 Chain B Binding Site BS02

Receptor Information
>1ky5 Chain B (length=430) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DKLPYKVADIGLAAWGRKALDIAENEMPGLMRMREMYSASKPLKGARIAG
CLHMTVETAVLIETLVALGAEVRWSSCNIFSTQDHAAAAIAKAGIPVFAW
KGETDEEYLWCIEQTLHFKDGPLNMILDDGGDLTNLIHTKHPQLLSGIRG
ISEETTTGVHNLYKMMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDG
IKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIEPINALQA
AMEGYEVTTMDEACKEGNIFVTTTGCVDIILGRHFEQMKDDAIVCNIGHF
DVEIDVKWLNENAVEKVNIKPQVDRYLLKNGHRIILLAEGRLVNLGCAMG
HPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKL
NVKLTKLTEKQAQYLGMPINGPFKPDHYRY
Ligand information
Ligand IDNAI
InChIInChI=1S/C21H29N7O14P2/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/h1,3-4,7-8,10-11,13-16,20-21,29-32H,2,5-6H2,(H2,23,33)(H,34,35)(H,36,37)(H2,22,24,25)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBOPGDPNILDQYTO-NNYOXOHSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=CCC(=C5)C(=O)N)O)O)O)O)N
CACTVS 3.341NC(=O)C1=CN(C=CC1)[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 1.5.0c1nc(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)N5C=CCC(=C5)C(=O)N)O)O)O)O)N
CACTVS 3.341NC(=O)C1=CN(C=CC1)[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
FormulaC21 H29 N7 O14 P2
Name1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE;
NADH
ChEMBLCHEMBL1234616
DrugBankDB00157
ZINCZINC000008215403
PDB chain1ky5 Chain B Residue 1432 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ky5 Catalytic Mechanism of S-adenosylhomocysteine hydrolase. Site-directed mutagenesis of Asp-130, Lys-185, Asp-189, and Asn-190.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		T1156 T1157 T1158 N1190 G1219 G1221 V1223 T1241 E1242 I1243 T1274 T1275 I1280 I1298 G1299 H1300 L1343 N1345 H1352
Binding residue
(residue number reindexed from 1)		T155 T156 T157 N189 G218 G220 V222 T240 E241 I242 T273 T274 I279 I297 G298 H299 L342 N344 H351
Annotation score2
Enzymatic activity
Enzyme Commision number 3.13.2.1: adenosylhomocysteinase.
Gene Ontology
Molecular Function
GO:0004013 adenosylhomocysteinase activity
GO:0005507 copper ion binding
GO:0016787 hydrolase activity
GO:0030554 adenyl nucleotide binding
GO:0042802 identical protein binding
GO:0051287 NAD binding
GO:0098604 adenosylselenohomocysteinase activity
Biological Process
GO:0001666 response to hypoxia
GO:0002439 chronic inflammatory response to antigenic stimulus
GO:0006730 one-carbon metabolic process
GO:0007584 response to nutrient
GO:0019510 S-adenosylhomocysteine catabolic process
GO:0033353 S-adenosylmethionine cycle
GO:0042745 circadian sleep/wake cycle
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005829 cytosol
GO:0042470 melanosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ky5, PDBe:1ky5, PDBj:1ky5
PDBsum1ky5
PubMed11927587
UniProtP10760|SAHH_RAT Adenosylhomocysteinase (Gene Name=Ahcy)

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