Structure of PDB 3n58 Chain A Binding Site BS03

Receptor Information
>3n58 Chain A (length=460) Species: 359391 (Brucella abortus 2308) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MVVKDISLADWGRKELDIAETEMPGLMAAREEFGKSQPLKGARISGSLHM
TIQTAVLIETLKVLGAEVRWASCNIFSTQDHAAAAIAATGTPVFAVKGET
LEEYWTYTDQIFQWPDGEPSNMILDDGGDATMYILIGARAEAGEDVLSNP
QSEEEEVLFAQIKKRMAATPGFFTKQRAAIKGVTEETTTGVNRLYQLQKK
GLLPFPAINVNDSVTKSKFDNKYGCKESLVDGIRRGTDVMMAGKVAVVCG
YGDVGKGSAQSLAGAGARVKVTEVDPICALQAAMDGFEVVTLDDAASTAD
IVVTTTGNKDVITIDHMRKMKDMCIVGNIGHFDNEIQVAALRNLKWTNVK
PQVDLIEFPDGKRLILLSEGRLLNLGNATGHPSFVMSASFTNQVLGQIEL
FTRTDAYKNEVYVLPKHLDEKVARLHLDKLGAKLTVLSEEQAAYIGVTPQ
GPFKSEHYRY
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 chain3n58 Chain B Residue 550 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3n58 Crystal structure of S-adenosyl-L-homocysteine hydrolase from brucella melitensis in ternary complex with NAD and adenosine, orthorhombic form
Resolution2.39 Å
Binding residue
(original residue number in PDB)		K460 Y464
Binding residue
(residue number reindexed from 1)		K454 Y458
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) H55 S78 S83 D132 E192 N217 K222 D226 N227 C231 H337 H387 S395 Q399
Catalytic site (residue number reindexed from 1) H49 S72 S77 D126 E186 N211 K216 D220 N221 C225 H331 H381 S389 Q393
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3n58, PDBe:3n58, PDBj:3n58
PDBsum3n58
PubMed
UniProtQ2YQX8|SAHH_BRUA2 Adenosylhomocysteinase (Gene Name=ahcY)

[Back to BioLiP]