Structure of PDB 5utu Chain H

Receptor sequence
>5utuH (length=487) Species: 353152 (Cryptosporidium parvum Iowa II) [Search protein sequence]
KMESRIKDISLAEFGLQDMEIAKTDMMGLVELQRKYRDSKPLKGARITGS
LHLTIETSVLVETLYELGAEIRWCSCNIYSTQDHAAAALVKKNIATVFAW
KNETIEDYWVCLNDAMTWRICGPNLIVDDGGDATLILHEGVKAEIEYEKY
NKIPEYLETELDENGKQLSMDLKCMYKVLKMELLKNPFRWRGMLKDLYGV
SEETTTGVLRLKIMESEGKLLLPAINVNDSVTKSKFDNTYGCRQSLLHGL
FNGCIQMLAGKKIVVLGYGEVGKGCAQGLSGVGARVIVTEIDPICALQAS
MEGYQVSVLEDVVSEADIFITATGNKDVITVEHMRKMKENAYIANIGHFD
DEIDVYGLENYPGIKVIEVKQNVHKFTFPDTQKSVILLCKGRLVNLGCAT
GHPPLVMSMSFTNQVLAQMDLWKSRELVDRSKNTRFFVKKLSKELDEYVA
RLHLDVLGIKLTKLTETQAKYINVSINGPYKSEDYRY
3D structure
PDB5utu 2.65 Angstrom Resolution Crystal Structure of S-adenosylhomocysteinase from Cryptosporidium parvum in Complex with SAH and NAD
ChainH
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) H52 S75 S80 D129 E203 N228 K233 D237 N238 C242 H348 H402 S410 Q414
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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