Structure of PDB 3rys Chain A

Receptor sequence
>3rysA (length=335) Species: 290340 (Paenarthrobacter aurescens TC1) [Search protein sequence]
TTSTAPPVAELHLHIEGTLQPELIFALAERNGIELPYEDIEELREKYEFT
DLQSFLDLYYANMAVLQTEQDFTDMTRAYLERAAAGGVRHAEIMMDPQAH
TSRGVALETCVNGVANALATSEEDFGVSTLLIAAFLRDMSEDSALEVLDQ
LLAMHAPIAGIGLDSAEVGNPPSKFERLYQRAAEAGLRRIAHAGEEGPAS
YITEALDVLHVERIDHGIRCMEDTDVVQRLVAEQVPLTVCPLSNVRLRAV
DKLADHPLPEMLAIGLNVCVNSDDPAYFGGYVDDNFEQLVKVLEFSVPEQ
ATLAANSIRSSFASDARKAVLLDEVTEWVKASVTP
3D structure
PDB3rys The crystal structure of adenine deaminase (AAur1117) from Arthrobacter aurescens
ChainA
Resolution2.601 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H19 H21 H199 E202 H223 D280
Catalytic site (residue number reindexed from 1) H12 H14 H192 E195 H216 D273
Enzyme Commision number 3.5.4.2: adenine deaminase.
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 ZN A H19 H21 H199 D280 H12 H14 H192 D273
BS02 ADE A H21 L59 L63 D171 S172 H199 E202 D280 D281 H14 L52 L56 D164 S165 H192 E195 D273 D274
Gene Ontology
Molecular Function
GO:0000034 adenine deaminase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0019239 deaminase activity
GO:0046872 metal ion binding
Biological Process
GO:0006146 adenine catabolic process
GO:0009117 nucleotide metabolic process
GO:0043103 hypoxanthine salvage
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:3rys, PDBe:3rys, PDBj:3rys
PDBsum3rys
PubMed
UniProtA1R3U3

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