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1MEE

THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0030435biological_processsporulation resulting in formation of a cellular spore
A0046872molecular_functionmetal ion binding
I0004867molecular_functionserine-type endopeptidase inhibitor activity
I0009611biological_processresponse to wounding
I0030414molecular_functionpeptidase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 400
ChainResidue
AGLN2
AASP41
ALEU75
AASN77
AILE79
AVAL81

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AALA169
ATYR171
ATHR174
AHOH458

site_idACT
Number of Residues3
DetailsENZYME ACTIVE SITE
ChainResidue
AASP32
AHIS64
ASER221

site_idCA1
Number of Residues6
DetailsSITE WITH STRONG AFFINITY FOR THE CALCIUM ION
ChainResidue
AGLN2
AASP41
ALEU75
AASN77
AILE79
AVAL81

site_idCA2
Number of Residues4
DetailsSITE WITH WEAK AFFINITY FOR THE CALCIUM ION
ChainResidue
AALA169
ATYR171
ATHR174
AHOH458

site_idRSB
Number of Residues2
DetailsBINDING SITE OF THE EGLIN-C INHIBITOR
ChainResidue
ILEU45
IASP46

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVIDSGIdssH
ChainResidueDetails
AVAL28-HIS39

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtIAA
ChainResidueDetails
AHIS64-ALA74

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAtPhVAG
ChainResidueDetails
AGLY219-GLY229

site_idPS00285
Number of Residues12
DetailsPOTATO_INHIBITOR Potato inhibitor I family signature. FPEVVGktVdqA
ChainResidueDetails
IPHE10-ALA21

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues269
DetailsDomain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Reactive bond"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1sca
ChainResidueDetails
ASER221
AHIS64
AASP32

246704

PDB entries from 2025-12-24

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