Structure of PDB 4yvf Chain B

Receptor sequence
>4yvfB (length=429) Species: 9606 (Homo sapiens) [Search protein sequence]
KLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGC
LHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWK
GETDEEYLWCIEQTLYFKDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGI
SEETTTGVHNLYKMMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGI
KRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAA
MEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFD
VEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGH
PSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLN
VKLTKLTEKQAQYLGMSCDGPFKPDHYRY
3D structure
PDB4yvf Discovery and structural analyses of S-adenosyl-L-homocysteine hydrolase inhibitors based on non-adenosine analogs.
ChainB
Resolution2.7 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) H52 S75 S80 D128 E153 N178 K183 D187 N188 C192 H298 H350 S358 Q362
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:4yvf, PDBe:4yvf, PDBj:4yvf
PDBsum4yvf
PubMed26037610
UniProtP23526|SAHH_HUMAN Adenosylhomocysteinase (Gene Name=AHCY)

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