Structure of PDB 5fbg Chain A

Receptor sequence
>5fbgA (length=267) Species: 510516 (Aspergillus oryzae RIB40) [Search protein sequence]
WGNLGHETVAYIAQSFVASSTESFCQNILGDDSTSYLANVATWANTYKYT
DAGEFSKPYHFIDAQDNPPQSCGVDYDRDCGSAGCSISAIQNYTNILLES
PNGSEALNALKFVVHIIGDIHQPLHDENLEAGGNGIDVTYDGETTNLHHI
WDTNMPEEAAGGYSLSVAKTYADLLTERIKTGTYSSKKDSWTDGIDIKDP
VSTSMIWAADANTYVCSTVLDDGLAYINSTDLSGEYYDKSQPVFEELIAK
AGYRLAAWLDLIASQPS
3D structure
PDB5fbg Structural and Catalytic Properties of S1 Nuclease from Aspergillus oryzae Responsible for Substrate Recognition, Cleavage, Non-Specificity, and Inhibition.
ChainA
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W21 H26 N65 K68 H80 H135 D139 H145 H168 D172
Catalytic site (residue number reindexed from 1) W1 H6 N45 K48 H60 H115 D119 H125 H148 D152
Enzyme Commision number 3.1.30.1: Aspergillus nuclease S1.
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 W21 H26 D139 W1 H6 D119
BS02 ZN A N65 H80 H135 D139 N45 H60 H115 D119
BS03 ZN A H145 H168 D172 H125 H148 D152
BS04 PO4 A N65 K68 H80 H135 D139 H145 N45 K48 H60 H115 D119 H125
BS05 DCZ A K68 F81 D83 H145 A151 N154 H168 K48 F61 D63 H125 A131 N134 H148
BS06 DCZ A E177 Y183 E157 Y163
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0004518 nuclease activity
GO:0004519 endonuclease activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0046872 metal ion binding
Biological Process
GO:0006308 DNA catabolic process
Cellular Component
GO:0005575 cellular_component

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5fbg, PDBe:5fbg, PDBj:5fbg
PDBsum5fbg
PubMed28036383
UniProtP24021|NUS1_ASPOR Nuclease S1 (Gene Name=nucS)

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