Structure of PDB 5fbg Chain B

Receptor sequence

>5fbgB (length=265) Species: 510516 (Aspergillus oryzae RIB40)

WGNLGHETVAYIAQSFVASSTESFCQNILGDDSTSYLANVATWANTYKYT
DAGEFSKPYHFIDAQDNPPQSCGVDYDRDCGSAGCSISAIQNYTNILLES
PNGSEALNALKFVVHIIGDIHQPLHDENLEAGGNGIDVTYDGETTNLHHI
WDTNMPEEAAGGYSLSVAKTYADLLTERIKTGTYSSKKDSWTDGIDIKDP
VSTSMIWAADANTYVCSTVLDDGLAYINSTDLSGEYYDKSQPVFEELIAK
AGYRLAAWLDLIASQ

3D structure

• PDB: 5fbg Structural and Catalytic Properties of S1 Nuclease from Aspergillus oryzae Responsible for Substrate Recognition, Cleavage, Non-Specificity, and Inhibition.
• Chain: B
• Resolution: 1.97 Å

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	B	W21 H26 D139	W1 H6 D119
BS02	ZN	B	H80 H135 D139	H60 H115 D119
BS03	ZN	B	H145 H168 D172	H125 H148 D152
BS04	PO4	B	W21 N65 K68 H80 H135 D139 H145 D172	W1 N45 K48 H60 H115 D119 H125 D152
BS05	GNG	B	F81 D83 H145 A151 N154 H168	F61 D63 H125 A131 N134 H148

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

External links

• PDB: RCSB:5fbg, PDBe:5fbg, PDBj:5fbg
• PDBsum: 5fbg
• PubMed: 28036383
• UniProt: P24021|NUS1_ASPOR Nuclease S1 (Gene Name=nucS)