Structure of PDB 1acc Chain A

Receptor sequence
>1accA (length=665) Species: 1392 (Bacillus anthracis) [Search protein sequence]
SSSQGLLGYYFSDLNFQAPMVVTSSTTGDLSIPSSELENIPSENQYFQSA
IWSGFIKVKKSDEYTFATSADNHVTMWVDDQEVINSNKIRLEKGRLYQIK
IQYQRENPTEKGLDFKLYWTDSQNKKEVISSDNLQLPELKQKSSVPDRDN
DGIPDSLEVEGYTVDVKNKRTFLSPWISNIHEKKGLTKYKSSPEKWSTAS
DPYSDFEKVTGRIDKNVSPEARHPLVAAYPIVHVDMENIILSKNETISKN
TSTSRTHTSEVVSAGFSNSNSSTVAIDHSLSLAGGLNTADTARLNANIRY
VNTGTAPIYNVLPTTSLVLGKNQTLATIKAKENQLSQILAPNNYYPSKNL
APIALNAQDDFSSTPITMNYNQFLELEKTKQLRLDTDQVYGNIATYNFEN
GRVRVDTGSNWSEVLPQIQETTARIIFNGKDLNLVERRIAAVNPSTTKPD
MTLKEALKIAFGFNEPNGNLQYQGKDITEFDFNFDQQTSQNIKNQLAELN
ATNIYTVLDKIKLNAKMNILIRDKRFHYDRNNIAVGADESVVKEAHREVI
NSSTEGLLLNIDKDIRKILSGYIVEIEDTEGLKEVINDRYDMLNISSLRQ
DGKTFIDFKKYNDKLPLYISNPNYKVNVYAVTKENTIINPSENGDTSTNG
IKKILIFSKKGYEIG
3D structure
PDB1acc Crystal structure of the anthrax toxin protective antigen.
ChainA
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 CA A D177 D179 D181 I183 E188 D147 D149 D151 I153 E158
BS02 CA A D179 D181 E188 S222 K225 D235 D149 D151 E158 S192 K195 D205
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0090729 toxin activity
Biological Process
GO:0043409 negative regulation of MAPK cascade
GO:0044533 positive regulation of apoptotic process in another organism
GO:0051260 protein homooligomerization
Cellular Component
GO:0005576 extracellular region
GO:0016020 membrane
GO:0020002 host cell plasma membrane
GO:0044164 host cell cytosol
GO:0044174 host cell endosome
GO:0044175 host cell endosome membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1acc, PDBe:1acc, PDBj:1acc
PDBsum1acc
PubMed9039918
UniProtP13423|PAG_BACAN Protective antigen (Gene Name=pagA)

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