Structure of PDB 3glq Chain A

Receptor sequence
>3glqA (length=462) Species: 320372 (Burkholderia pseudomallei 1710b) [Search protein sequence]
QDYVVADIALAGWGRKELNIAETEMPGLVQIRDEYKAQQPLKGARIAGSL
HMTIQTGVLIETLKALGADVRWASCNIFSTQDHAAAAIVEAGTPVFAFKG
ESLDEYWEFSHRIFEWPNGEFANMILDDGGDATLLLILGSKAEKDRSVIA
RPTNEEEVALFKSIERHLEIDGSWYSKRLAHIKGVTEETTTGVHRLYQME
KDGRLPFPAFNVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKIAVV
AGYGDVGKGCAQSLRGLGATVWVTEIDPICALQAAMEGYRVVTMEYAADK
ADIFVTATGNYHVINHDHMKAMRHNAIVCNIGHFDSEIDVASTRQYQWEN
IKPQVDHIIFPDGKRVILLAEGRLVNLGCATGHPSFVMSNSFTNQTLAQI
ELFTRGGEYANKVYVLPKHLDEKVARLHLARIGAQLSELSDDQAAYIGVS
KAGPFKPDHYRY
3D structure
PDB3glq Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia pseudomallei in complex with 9-beta-D-arabino-furansyl-adenine
ChainA
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) H62 S85 S90 D139 E199 N224 K229 D233 N234 C238 H344 H394 S402 Q406
Catalytic site (residue number reindexed from 1) H51 S74 S79 D128 E188 N213 K218 D222 N223 C227 H333 H383 S391 Q395
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:3glq, PDBe:3glq, PDBj:3glq
PDBsum3glq
PubMed
UniProtQ3JY79|SAHH_BURP1 Adenosylhomocysteinase (Gene Name=ahcY)

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