Structure of PDB 3nj4 Chain D

Receptor sequence
>3nj4D (length=430) Species: 9606 (Homo sapiens) [Search protein sequence]
DKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAG
CLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAW
KGETDEEYLWCIEQTLYFKDGPLNMILDDGGDLTNLIHTKYPQLLPGIRG
ISEETTTGVHNLYKMMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDG
IKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQA
AMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHF
DVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMG
HPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKL
NVKLTKLTEKQAQYLGMSCDGPFKPDHYRY
3D structure
PDB3nj4 X-ray crystal structure and binding mode analysis of human S-adenosylhomocysteine hydrolase complexed with novel mechanism-based inhibitors, haloneplanocin A analogues.
ChainD
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H55 S78 S83 D131 E156 N181 K186 D190 N191 C195 H301 H353 S361 Q365
Catalytic site (residue number reindexed from 1) H53 S76 S81 D129 E154 N179 K184 D188 N189 C193 H299 H351 S359 Q363
Enzyme Commision number 3.13.2.1: adenosylhomocysteinase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004013 adenosylhomocysteinase activity
GO:0005515 protein binding
GO:0016787 hydrolase activity
Biological Process
GO:0006730 one-carbon metabolic process
GO:0033353 S-adenosylmethionine cycle
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005829 cytosol
GO:0042470 melanosome
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3nj4, PDBe:3nj4, PDBj:3nj4
PDBsum3nj4
PubMed21226494
UniProtP23526|SAHH_HUMAN Adenosylhomocysteinase (Gene Name=AHCY)

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