Structure of PDB 5utu Chain G

Receptor sequence
>5utuG (length=495) Species: 353152 (Cryptosporidium parvum Iowa II) [Search protein sequence]
YKMESRIKDISLAEFGLQDMEIAKTDMMGLVELQRKYRDSKPLKGARITG
SLHLTIETSVLVETLYELGAEIRWCSCNIYSTQDHAAAALVKKNIATVFA
WKNETIEDYWVCLNDAMTWRNPNDKDKICGPNLIVDDGGDATLILHEGVK
AEIEYEKYNKIPEYLETELDENGKQLSMDLKCMYKVLKMELLKNPFRWRG
MLKDLYGVSEETTTGVLRLKIMESEGKLLLPAINVNDSVTKSKFDNTYGC
RQSLLHGLFNGCIQMLAGKKIVVLGYGEVGKGCAQGLSGVGARVIVTEID
PICALQASMEGYQVSVLEDVVSEADIFITATGNKDVITVEHMRKMKENAY
IANIGHFDDEIDVYGLENYPGIKVIEVKQNVHKFTFPDTQKSVILLCKGR
LVNLGCATGHPPLVMSMSFTNQVLAQMDLWKSRELVDRSKNTRFFVKKLS
KELDEYVARLHLDVLGIKLTKLTETQAKYINVSINGPYKSEDYRY
3D structure
PDB5utu 2.65 Angstrom Resolution Crystal Structure of S-adenosylhomocysteinase from Cryptosporidium parvum in Complex with SAH and NAD
ChainG
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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) H53 S76 S81 D137 E211 N236 K241 D245 N246 C250 H356 H410 S418 Q422
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:5utu, PDBe:5utu, PDBj:5utu
PDBsum5utu
PubMed
UniProtQ5CPH1

[Back to BioLiP]