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1DEU

CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN X: A CYSTEINE PROTEASE WITH THE PROREGION COVALENTLY LINKED TO THE ACTIVE SITE CYSTEINE

Functional Information from GO Data
ChainGOidnamespacecontents
A0002003biological_processangiotensin maturation
A0004180molecular_functioncarboxypeptidase activity
A0004197molecular_functioncysteine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005764cellular_componentlysosome
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005886cellular_componentplasma membrane
A0005938cellular_componentcell cortex
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
A0010757biological_processnegative regulation of plasminogen activation
A0030134cellular_componentCOPII-coated ER to Golgi transport vesicle
A0031410cellular_componentcytoplasmic vesicle
A0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
A0035580cellular_componentspecific granule lumen
A0043231cellular_componentintracellular membrane-bounded organelle
A0051603biological_processproteolysis involved in protein catabolic process
A0060441biological_processepithelial tube branching involved in lung morphogenesis
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A1904813cellular_componentficolin-1-rich granule lumen
B0002003biological_processangiotensin maturation
B0004180molecular_functioncarboxypeptidase activity
B0004197molecular_functioncysteine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005764cellular_componentlysosome
B0005783cellular_componentendoplasmic reticulum
B0005788cellular_componentendoplasmic reticulum lumen
B0005886cellular_componentplasma membrane
B0005938cellular_componentcell cortex
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
B0010757biological_processnegative regulation of plasminogen activation
B0030134cellular_componentCOPII-coated ER to Golgi transport vesicle
B0031410cellular_componentcytoplasmic vesicle
B0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
B0035580cellular_componentspecific granule lumen
B0043231cellular_componentintracellular membrane-bounded organelle
B0051603biological_processproteolysis involved in protein catabolic process
B0060441biological_processepithelial tube branching involved in lung morphogenesis
B0062023cellular_componentcollagen-containing extracellular matrix
B0070062cellular_componentextracellular exosome
B1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvRNSWgepWGerGWLrI
ChainResidueDetails
ATYR195-ILE214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:10656802, ECO:0000305|PubMed:10745011
ChainResidueDetails
ACYS31
AHIS180
AASN200
BCYS31
BHIS180
BASN200

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN123
BASN123

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN163
BASN163

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
ACYS31
AASN200
AHIS180

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BCYS31
BASN200
BHIS180

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AGLN22
ACYS31
AHIS180

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BGLN22
BCYS31
BHIS180

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AGLN22
AASN200
AHIS180

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BGLN22
BASN200
BHIS180

site_idMCSA1
Number of Residues4
DetailsM-CSA 953
ChainResidueDetails
AGLN22electrostatic stabiliser
ACYS31covalent catalysis, proton shuttle (general acid/base)
AHIS180proton shuttle (general acid/base)
AASN200electrostatic stabiliser, modifies pKa

site_idMCSA2
Number of Residues4
DetailsM-CSA 953
ChainResidueDetails
BGLN22electrostatic stabiliser
BCYS31covalent catalysis, proton shuttle (general acid/base)
BHIS180proton shuttle (general acid/base)
BASN200electrostatic stabiliser, modifies pKa

223532

PDB entries from 2024-08-07

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