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1YU6

Crystal Structure of the Subtilisin Carlsberg:OMTKY3 Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
C0004867molecular_functionserine-type endopeptidase inhibitor activity
C0005576cellular_componentextracellular region
C0030414molecular_functionpeptidase inhibitor activity
C0140678molecular_functionmolecular function inhibitor activity
D0004867molecular_functionserine-type endopeptidase inhibitor activity
D0005576cellular_componentextracellular region
D0030414molecular_functionpeptidase inhibitor activity
D0140678molecular_functionmolecular function inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AGLN2
AASP41
ALEU75
AASN77
ATHR79
AVAL81

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 402
ChainResidue
BASN77
BTHR79
BVAL81
BGLN2
BASP41
BLEU75

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

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

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

site_idPS00282
Number of Residues23
DetailsKAZAL_1 Kazal serine protease inhibitors family signature. CnkalNpvCgTdgvtYdneCvl.C
ChainResidueDetails
CCYS-43-CYS-21
CCYS16-CYS38

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues536
DetailsDomain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8512925","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Reactive bond 3 for chymotrypsin, elastase, proteases A and B, and subtilisin"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

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

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1sca
ChainResidueDetails
BSER221
BHIS64
BASP32

247536

PDB entries from 2026-01-14

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