Structure of PDB 1ak0 Chain A Binding Site BS04
Receptor Information
>1ak0 Chain A (length=264) Species:
5077
(Penicillium citrinum) [
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WGALGHATVAYVAQHYVSPEAASWAQGILGSSSSSYLASIASWADEYRLT
SAGKWSASLHFIDAEDNPPTNCNVDYERDCGSSGCSISAIANYTQRVSDS
SLSSENHAEALRFLVHFIGDMTQPLHDEAYAVGGNKINVTFDGYHDNLHS
DWDTYMPQKLIGGHALSDAESWAKTLVQNIESGNYTAQAIGWIKGDNISE
PITTATRWASDANALVCTVVMPHGAAALQTGDLYPTYYDSVIDTIELQIA
KGGYRLANWINEIH
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1ak0 Chain A Residue 274 [
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Receptor-Ligand Complex Structure
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PDB
1ak0
Recognition of single-stranded DNA by nuclease P1: high resolution crystal structures of complexes with substrate analogs.
Resolution
1.8 Å
Binding residue
(original residue number in PDB)
H15 E181
Binding residue
(residue number reindexed from 1)
H15 E181
Annotation score
4
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.
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
PDBsum
1ak0
PubMed
9726413
UniProt
P24289
|NUP1_PENCI Nuclease P1
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