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4MWT

Crystal structure of human PPCA (trigonal crystal form 2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0004185molecular_functionserine-type carboxypeptidase activity
A0005576cellular_componentextracellular region
A0005764cellular_componentlysosome
A0005783cellular_componentendoplasmic reticulum
A0006508biological_processproteolysis
A0006886biological_processintracellular protein transport
A0008047molecular_functionenzyme activator activity
A0016020cellular_componentmembrane
A0031647biological_processregulation of protein stability
A0035578cellular_componentazurophil granule lumen
A0043202cellular_componentlysosomal lumen
A0043231cellular_componentintracellular membrane-bounded organelle
A0070062cellular_componentextracellular exosome
A0098575cellular_componentlumenal side of lysosomal membrane
A1904714biological_processregulation of chaperone-mediated autophagy
A1904715biological_processnegative regulation of chaperone-mediated autophagy
B0004180molecular_functioncarboxypeptidase activity
B0004185molecular_functionserine-type carboxypeptidase activity
B0005576cellular_componentextracellular region
B0005764cellular_componentlysosome
B0005783cellular_componentendoplasmic reticulum
B0006508biological_processproteolysis
B0006886biological_processintracellular protein transport
B0008047molecular_functionenzyme activator activity
B0016020cellular_componentmembrane
B0031647biological_processregulation of protein stability
B0035578cellular_componentazurophil granule lumen
B0043202cellular_componentlysosomal lumen
B0043231cellular_componentintracellular membrane-bounded organelle
B0070062cellular_componentextracellular exosome
B0098575cellular_componentlumenal side of lysosomal membrane
B1904714biological_processregulation of chaperone-mediated autophagy
B1904715biological_processnegative regulation of chaperone-mediated autophagy
Functional Information from PROSITE/UniProt
site_idPS00131
Number of Residues8
DetailsCARBOXYPEPT_SER_SER Serine carboxypeptidases, serine active site. LtGESYAG
ChainResidueDetails
ALEU146-GLY153

site_idPS00560
Number of Residues18
DetailsCARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. IafLtIkGAGHmVPtdkP
ChainResidueDetails
AILE419-PRO436

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE:
ChainResidueDetails
BSER150
ASER150

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ATYR402
BTYR402

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN117
BASN117

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN335
BASN335

221051

PDB entries from 2024-06-12

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