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6A4R

Crystal structure of aspartate bound peptidase E from Salmonella enterica

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0016805molecular_functiondipeptidase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0016787molecular_functionhydrolase activity
B0016805molecular_functiondipeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue ASP A 301
ChainResidue
AGLY87
AHIS157
AHOH416
BGLU169
AGLY88
ASER120
AALA121
AASN124
ATHR133
AASN134
AASP135
APRO156

site_idAC2
Number of Residues12
Detailsbinding site for residue ASP B 301
ChainResidue
AGLU169
BGLY87
BGLY88
BSER120
BALA121
BASN124
BTHR133
BASN134
BASP135
BPRO156
BHIS157
BHOH428

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"10762256","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 599
ChainResidueDetails
AGLY88electrostatic stabiliser
ASER120covalent catalysis
AALA121electrostatic stabiliser
AHIS157proton shuttle (general acid/base)
AGLU192electrostatic stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 599
ChainResidueDetails
BGLY88electrostatic stabiliser
BSER120covalent catalysis
BALA121electrostatic stabiliser
BHIS157proton shuttle (general acid/base)
BGLU192electrostatic stabiliser

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PDB entries from 2025-07-16

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