Structure of PDB 4pfj Chain B

Receptor sequence
>4pfjB (length=427) Species: 9606 (Homo sapiens) [Search protein sequence]
PYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLH
MTVETAVLIETLVTLGAEVQWSSCNIFSTQNHAAAAIAKAGIPVYAWKGE
TDEEYLWCIEQTLYFKDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISE
ETTTGVHNLYKMMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKR
ATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAME
GYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVE
IDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPS
FVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVACAHLGKLNVK
LTKLTEKQAQYLGMSCDGPFKPDHYRY
3D structure
PDB4pfj Regulation of s-adenosylhomocysteine hydrolase by lysine acetylation.
ChainB
Resolution2.3 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) H50 S73 S78 D126 E151 N176 K181 D185 N186 C190 H296 H348 S356 Q360
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:4pfj, PDBe:4pfj, PDBj:4pfj
PDBsum4pfj
PubMed25248746
UniProtP23526|SAHH_HUMAN Adenosylhomocysteinase (Gene Name=AHCY)

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