Structure of PDB 1ak0 Chain A

Receptor sequence
>1ak0A (length=264) Species: 5077 (Penicillium citrinum) [Search protein sequence]
WGALGHATVAYVAQHYVSPEAASWAQGILGSSSSSYLASIASWADEYRLT
SAGKWSASLHFIDAEDNPPTNCNVDYERDCGSSGCSISAIANYTQRVSDS
SLSSENHAEALRFLVHFIGDMTQPLHDEAYAVGGNKINVTFDGYHDNLHS
DWDTYMPQKLIGGHALSDAESWAKTLVQNIESGNYTAQAIGWIKGDNISE
PITTATRWASDANALVCTVVMPHGAAALQTGDLYPTYYDSVIDTIELQIA
KGGYRLANWINEIH
3D structure
PDB1ak0 Recognition of single-stranded DNA by nuclease P1: high resolution crystal structures of complexes with substrate analogs.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W1 H6 D45 R48 H60 H116 D120 H126 H149 D153
Catalytic site (residue number reindexed from 1) W1 H6 D45 R48 H60 H116 D120 H126 H149 D153
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 H60 H116 D120 H60 H116 D120
BS02 ZN A H126 H149 D153 H126 H149 D153
BS03 ZN A W1 H6 D120 W1 H6 D120
BS04 ZN A H15 E181 H15 E181
BS05 THS A F61 D63 N135 H149 F61 D63 N135 H149
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
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:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ak0, PDBe:1ak0, PDBj:1ak0
PDBsum1ak0
PubMed9726413
UniProtP24289|NUP1_PENCI Nuclease P1

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