Structure of PDB 5utu Chain E

Receptor sequence
>5utuE (length=494) Species: 353152 (Cryptosporidium parvum Iowa II) [Search protein sequence]
AYKMESRIKDISLAEFGLQDMEIAKTDMMGLVELQRKYRDSKPLKGARIT
GSLHLTIETSVLVETLYELGAEIRWCSCNIYSTQDHAAAALVKKNIATVF
AWKNETIEDYWVCLNDAMTWRNPNDKICGPNLIVDDGGDATLILHEGVKA
EIEYEKYNKIPEYLETELDENGKQLSMDLKCMYKVLKMELLKNPFRWRGM
LKDLYGVSEETTTGVLRLKIMESEGKLLLPAINVNDSVTKSKFDNTYGCR
QSLLHGLFNGCIQMLAGKKIVVLGYGEVGKGCAQGLSGVGARVIVTEIDP
ICALQASMEGYQVSVLEDVVSEADIFITATGNKDVITVEHMRKMKENAYI
ANIGHFDDEIDVYGLENYPGIKVIEVKQNVHKFTFPDTQKSVILLCKGRL
VNLGCATGHPPLVMSMSFTNQVLAQMDLWKSRELVDRSKNTRFFVKKLSK
ELDEYVARLHLDVLGIKLTKLTETQAKYINVSINGPYKSEDYRY
3D structure
PDB5utu 2.65 Angstrom Resolution Crystal Structure of S-adenosylhomocysteinase from Cryptosporidium parvum in Complex with SAH and NAD
ChainE
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H53 S76 S81 D137 E211 N236 K241 D245 N246 C250 H356 H410 S418 Q422
Catalytic site (residue number reindexed from 1) H54 S77 S82 D136 E210 N235 K240 D244 N245 C249 H355 H409 S417 Q421
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:5utu, PDBe:5utu, PDBj:5utu
PDBsum5utu
PubMed
UniProtQ5CPH1

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