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4C2H

Crystal structure of the CtpB(V118Y) mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0006508biological_processproteolysis
A0006518biological_processpeptide metabolic process
A0007165biological_processsignal transduction
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0030435biological_processsporulation resulting in formation of a cellular spore
A0042277molecular_functionpeptide binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
B0004175molecular_functionendopeptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0006508biological_processproteolysis
B0006518biological_processpeptide metabolic process
B0007165biological_processsignal transduction
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0030435biological_processsporulation resulting in formation of a cellular spore
B0042277molecular_functionpeptide binding
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:24243021
ChainResidueDetails
ASER309
BSER309

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:24243021
ChainResidueDetails
ALYS334
AGLN338
BLYS334
BGLN338

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Crucial for substrate binding and protease activation => ECO:0000269|PubMed:24243021
ChainResidueDetails
AARG168
BARG168

226707

PDB entries from 2024-10-30

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