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3S0X

The crystal structure of GxGD membrane protease FlaK

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016020cellular_componentmembrane
B0004190molecular_functionaspartic-type endopeptidase activity
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMSE501
ALEU547-ASP549
AVAL590-VAL610
APRO717-PHE730
BMSE501
BLEU547-ASP549
BVAL590-VAL610
BPRO717-PHE730

site_idSWS_FT_FI2
Number of Residues218
DetailsTRANSMEM: Helical => ECO:0000305
ChainResidueDetails
AILE502-ASP518
BASP579-LEU589
BPRO611-ASN639
BLEU705-THR716
AILE524-THR546
ATYR550-LEU572
AASP579-LEU589
APRO611-ASN639
ALEU705-THR716
BILE502-ASP518
BILE524-THR546
BTYR550-LEU572

site_idSWS_FT_FI3
Number of Residues146
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
APHE519-GLU523
ASER573-GLY578
AGLY640-PRO704
BPHE519-GLU523
BSER573-GLY578
BGLY640-PRO704

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Essential for catalysis => ECO:0000250
ChainResidueDetails
AASP518
AASP579
BASP518
BASP579

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PDB entries from 2024-07-31

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