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2SEC

STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO

Replaces:  1SEC
Functional Information from GO Data
ChainGOidnamespacecontents
E0004252molecular_functionserine-type endopeptidase activity
E0006508biological_processproteolysis
E0008236molecular_functionserine-type peptidase activity
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 E 276
ChainResidue
EGLN2
EASP41
ELEU75
EASN77
ETHR79
EVAL81

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA E 277
ChainResidue
EALA169
ETYR171
EVAL174
EHOH361
EHOH430

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA E 278
ChainResidue
EALA37
EHIS39
ELEU42

site_idACT
Number of Residues3
Detailscatalytic site
ChainResidue
EASP32
EHIS64
ESER221

site_idIO1
Number of Residues6
Detailsion binding site
ChainResidue
EGLN2
EASP41
ELEU75
EASN77
ETHR79
EVAL81

site_idIO2
Number of Residues5
Detailsion binding site
ChainResidue
EALA169
ETYR171
EVAL174
EHOH361
EHOH430

site_idIO3
Number of Residues5
Detailsion binding site
ChainResidue
EALA37
EHIS39
ELEU42
EHOH373
EHOH463

site_idRSB
Number of Residues2
Detailsinhibitor reactive site
ChainResidue
ILEU59
IASP60

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIqasH
ChainResidueDetails
EVAL28-HIS39

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA
ChainResidueDetails
EHIS64-ALA74

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG
ChainResidueDetails
EGLY219-GLY229

site_idPS00285
Number of Residues12
DetailsPOTATO_INHIBITOR Potato inhibitor I family signature. FPEVVGktVdqA
ChainResidueDetails
IPHE24-ALA35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues268
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: {"evidences":[{"source":"PubMed","id":"8512925","evidenceCode":"ECO:0000269"}]}
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
ESER221
EHIS64
EASP32

239803

PDB entries from 2025-08-06

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