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7Y5Q

Structure of 1:1 PAPP-A.STC2 complex(half map)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004222molecular_functionmetalloendopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0006974biological_processDNA damage response
A0007166biological_processcell surface receptor signaling pathway
A0007565biological_processfemale pregnancy
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0008643biological_processcarbohydrate transport
A0015144molecular_functioncarbohydrate transmembrane transporter activity
A0015768biological_processmaltose transport
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0034219biological_processcarbohydrate transmembrane transport
A0034289biological_processdetection of maltose stimulus
A0042597cellular_componentperiplasmic space
A0042956biological_processmaltodextrin transmembrane transport
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0046872molecular_functionmetal ion binding
A0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
A0055085biological_processtransmembrane transport
A0060326biological_processcell chemotaxis
A1901982molecular_functionmaltose binding
A1990060cellular_componentmaltose transport complex
B0004175molecular_functionendopeptidase activity
B0004222molecular_functionmetalloendopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006508biological_processproteolysis
B0006974biological_processDNA damage response
B0007166biological_processcell surface receptor signaling pathway
B0007565biological_processfemale pregnancy
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0008643biological_processcarbohydrate transport
B0015144molecular_functioncarbohydrate transmembrane transporter activity
B0015768biological_processmaltose transport
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0034219biological_processcarbohydrate transmembrane transport
B0034289biological_processdetection of maltose stimulus
B0042597cellular_componentperiplasmic space
B0042956biological_processmaltodextrin transmembrane transport
B0043190cellular_componentATP-binding cassette (ABC) transporter complex
B0046872molecular_functionmetal ion binding
B0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
B0055085biological_processtransmembrane transport
B0060326biological_processcell chemotaxis
B1901982molecular_functionmaltose binding
B1990060cellular_componentmaltose transport complex
C0005179molecular_functionhormone activity
C0005576cellular_componentextracellular region
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TMIHEIGHSL
ChainResidueDetails
ATHR479-LEU488

site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
APRO-275-ASN-258

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues61
DetailsDomain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues67
DetailsDomain: {"description":"Sushi 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12421832","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues21
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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