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6I58

Allosteric activation of human prekallikrein by apple domain disc rotation

Replaces:  2F83
Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0007596biological_processblood coagulation
A0008201molecular_functionheparin binding
A0008236molecular_functionserine-type peptidase activity
A0016020cellular_componentmembrane
A0030193biological_processregulation of blood coagulation
A0031639biological_processplasminogen activation
A0051919biological_processpositive regulation of fibrinolysis
A0070009molecular_functionserine-type aminopeptidase activity
A0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU409-CYS414

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAckGDSGGPLS
ChainResidueDetails
AASP551-SER562

site_idPS00495
Number of Residues84
DetailsAPPLE Apple domain. CvtqLlkdtcFeggDIttvftpsakyCqvvCTyhprClLFtFtaespsedptrwftCvLKdSvtetlprvnrtaai.SGySFkqC
ChainResidueDetails
ACYS2-CYS85
ACYS92-CYS175
ACYS182-CYS265
ACYS273-CYS356

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS413
AASP462
ASER557

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS529

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:25092234
ChainResidueDetails
AASN72

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:25092234
ChainResidueDetails
AASN108

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; atypical => ECO:0000269|PubMed:25092234
ChainResidueDetails
AASN145

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:25092234
ChainResidueDetails
AASN432

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:1998667, ECO:0000269|PubMed:25092234
ChainResidueDetails
AASN473

226707

PDB entries from 2024-10-30

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