Structure of PDB 3n58 Chain D

Receptor sequence
>3n58D (length=461) Species: 359391 (Brucella abortus 2308) [Search protein sequence]
SMVVKDISLADWGRKELDIAETEMPGLMAAREEFGKSQPLKGARISGSLH
MTIQTAVLIETLKVLGAEVRWASCNIFSTQDHAAAAIAATGTPVFAVKGE
TLEEYWTYTDQIFQWPDGEPSNMILDDGGDATMYILIGARAEAGEDVLSN
PQSEEEEVLFAQIKKRMAATPGFFTKQRAAIKGVTEETTTGVNRLYQLQK
KGLLPFPAINVNDSVTKSKFDNKYGCKESLVDGIRRGTDVMMAGKVAVVC
GYGDVGKGSAQSLAGAGARVKVTEVDPICALQAAMDGFEVVTLDDAASTA
DIVVTTTGNKDVITIDHMRKMKDMCIVGNIGHFDNEIQVAALRNLKWTNV
KPQVDLIEFPDGKRLILLSEGRLLNLGNATGHPSFVMSASFTNQVLGQIE
LFTRTDAYKNEVYVLPKHLDEKVARLHLDKLGAKLTVLSEEQAAYIGVTP
QGPFKSEHYRY
3D structure
PDB3n58 Crystal structure of S-adenosyl-L-homocysteine hydrolase from brucella melitensis in ternary complex with NAD and adenosine, orthorhombic form
ChainD
Resolution2.39 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 D132 E192 N217 K222 D226 N227 C231 H337 H387 S395 Q399
Catalytic site (residue number reindexed from 1) H50 S73 S78 D127 E187 N212 K217 D221 N222 C226 H332 H382 S390 Q394
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:3n58, PDBe:3n58, PDBj:3n58
PDBsum3n58
PubMed
UniProtQ2YQX8|SAHH_BRUA2 Adenosylhomocysteinase (Gene Name=ahcY)

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