Structure of PDB 6uk3 Chain C

Receptor sequence
>6uk3C (length=475) Species: 1257118 (Acanthamoeba castellanii str. Neff) [Search protein sequence]
TQTQTQPAGNAFQYEIRDISLAEFGRKEINLAEHEMPGLMQTREKYGAEQ
PLKGVRLAGSLHMTIQTAVLIETLQALGANVRWCSCNIFSTQDHAAAAIV
AAGTPVFAWKGETLEEYWECTWKTLLFPDDMGPQLIVDDGGDATLMVHRG
FYAEDNPSILDDDEGSEELAIVNKLLKRIQKEKPGYWHKIVPELKGVSEE
TTTGVHRLYEMMKEGKLLFPALNVNDSVTKSKFDNVYGCRHSLVDAIMRA
TDVMLSGKVACVLGYGDVGKGSAESLKGQGARVVVTEVDPICALQACMAG
YEVVRIEDVLDKAEIFVTTTGNCDIIRIEHMEKMRHNAIVCNIGHFDNEI
QVKALKEFPGIKRIEIKPQVDQFVFPDGHAIVLLAEGRLVNLGCATGHPS
FVMSNSFTNQTLAQISLWKEKYELGVYTLPKKLDEEVARLHLEKLGAKLT
VLTDKQAKYLGIAKDGPYKPDHYRY
3D structure
PDB6uk3 Crystal Structure of S-adenosyl-L-homocysteine hydrolase from Acanthamoeba castellanii with bound NAD and Adenosine
ChainC
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H64 S87 S92 D141 E202 N227 K232 D236 N237 C241 H347 H400 S408 Q412
Catalytic site (residue number reindexed from 1) H62 S85 S90 D139 E200 N225 K230 D234 N235 C239 H345 H398 S406 Q410
Enzyme Commision number 3.13.2.1: adenosylhomocysteinase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004013 adenosylhomocysteinase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006730 one-carbon metabolic process
GO:0033353 S-adenosylmethionine cycle
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6uk3, PDBe:6uk3, PDBj:6uk3
PDBsum6uk3
PubMed
UniProtL8H6B5

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