Structure of PDB 3n58 Chain B

Receptor sequence

>3n58B (length=461) Species: 359391 (Brucella abortus 2308)

SMVVKDISLADWGRKELDIAETEMPGLMAAREEFGKSQPLKGARISGSLH
MTIQTAVLIETLKVLGAEVRWASCNIFSTQDHAAAAIAATGTPVFAVKGE
TLEEYWTYTDQIFQWPDGEPSNMILDDGGDATMYILIGARAEAGEDVLSN
PQSEEEEVLFAQIKKRMAATPGFFTKQRAAIKGVTEETTTGVNRLYQLQK
KGLLPFPAINVNDSVTKSKFDNKYGCKESLVDGIRRGTDVMMAGKVAVVC
GYGDVGKGSAQSLAGAGARVKVTEVDPICALQAAMDGFEVVTLDDAASTA
DIVVTTTGNKDVITIDHMRKMKDMCIVGNIGHFDNEIQVAALRNLKWTNV
KPQVDLIEFPDGKRLILLSEGRLLNLGNATGHPSFVMSASFTNQVLGQIE
LFTRTDAYKNEVYVLPKHLDEKVARLHLDKLGAKLTVLSEEQAAYIGVTP
QGPFKSEHYRY

3D structure

• PDB: 3n58 Crystal structure of S-adenosyl-L-homocysteine hydrolase from brucella melitensis in ternary complex with NAD and adenosine, orthorhombic form
• Chain: B
• Resolution: 2.39 Å

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

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	NAD	B	K460 Y464	K455 Y459
BS02	NAD	B	N227 G258 D259 V260 E279 V280 T311 T312 I335 G336 H337 N380 H387	N222 G253 D254 V255 E274 V275 T306 T307 I330 G331 H332 N375 H382

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

External links

• PDB: RCSB:3n58, PDBe:3n58, PDBj:3n58
• PDBsum: 3n58
• UniProt: Q2YQX8|SAHH_BRUA2 Adenosylhomocysteinase (Gene Name=ahcY)