Structure of PDB 6f3o Chain D

Receptor sequence
>6f3oD (length=461) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
GFTDYKVADITLAAWGRRELIIAESEMPALMGLRRKYAGQQPLKGAKILG
CIHMTIQTGVLIETLVALGAEVRWSSCNIFSTQDQAAAAIAAAGIPVFAW
KGETEEEYEWCIEQTILKDGQPWDANMVLDDGGDLTEILHKKYPQMLERI
HGITEETTTGVHRLLDMLKNGTLKVPAINVNDSVTKSKNDNKYGCRHSLN
DAIKRGTDHLLSGKQALVIGYGDVGKGSSQSLRQEGMIVKVAEVDPICAM
QACMDGFEVVSPYKNGINDGTEASIDAALLGKIDLIVTTTGNVNVCDANM
LKALKKRAVVCNIGHFDNEIDTAFMRKNWAWEEVKPQVHKIHRTGKDGFD
AHNDDYLILLAEGRLVNLGNATGHPSRIMDGSFANQVLAQIHLFEQKYAD
LPAAEKAKRLSVEVLPKKLDEEVALEMVKGFGGVVTQLTPKQAEYIGVSV
EGPFKPDTYRY
3D structure
PDB6f3o Metal-cation regulation of enzyme dynamics is a key factor influencing the activity of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa.
ChainD
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H61 S84 S89 D139 E164 N189 K194 D198 N199 C203 H323 H382 S390 Q394
Catalytic site (residue number reindexed from 1) H53 S76 S81 D131 E156 N181 K186 D190 N191 C195 H315 H374 S382 Q386
Enzyme Commision number 3.13.2.1: adenosylhomocysteinase.
Interaction with ligand
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6f3o, PDBe:6f3o, PDBj:6f3o
PDBsum6f3o
PubMed30054521
UniProtQ9I685|SAHH_PSEAE Adenosylhomocysteinase (Gene Name=ahcY)

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