Structure of PDB 6oha Chain A

Receptor sequence
>6ohaA (length=451) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
DKHGKFLVFFGTFVDTPKLGELRIREKTSVGVLNGIIRFVNRNSLDPVKD
CLDHDSSLSPEDVTVVDINNSFYFPGFVDTHNHVSQYPNVGVFGNSTLLD
WLEKYTFPIEAALANENIAREVYNKVISKTLSHGTTTVAYYNTIDLKSTK
LLAQLSSLLGQRVLVGKVCMDTNGPEYYIEDTKTSFESTVKVVKYIRETI
CDPLVNPIVTPRFAPSCSRELMQQLSKLVKDENIHVQTHLSENKEEIQWV
QDLFPECESYTDVYDKYGLLTEKTVLAHCIHLTDAEARVIKQRRCGISHC
PISNSSLTSGECRVRWLLDQGIKVGLGTDVSAGHSCSILTTGRQAFAVSR
HLAMRETDHAKLSVSECLFLATMGGAQVLRMDETLGTFDVGKQFDAQMID
TNAPGSNVDMFHWQLNPPLLTNEDIIAKWFFNGDDRNTTKVWVAGQQVYQ
I
3D structure
PDB6oha Structural Determinants for Substrate Selectivity in Guanine Deaminase Enzymes of the Amidohydrolase Superfamily.
ChainA
Resolution2.21 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.4.3: guanine 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 XAN A H102 L117 W120 R231 F232 H258 E261 H297 D348 H83 L98 W101 R212 F213 H239 E242 H278 D329
BS02 ZN A H100 H102 H258 D348 H81 H83 H239 D329
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008892 guanine deaminase activity
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0046872 metal ion binding
Biological Process
GO:0006147 guanine catabolic process
GO:0046098 guanine metabolic process
Cellular Component
GO:0005737 cytoplasm
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:6oha, PDBe:6oha, PDBj:6oha
PDBsum6oha
PubMed31283204
UniProtQ07729|GUAD_YEAST Probable guanine deaminase (Gene Name=GUD1)

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