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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
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0008643biological_processcarbohydrate transport
A0015144molecular_functioncarbohydrate transmembrane transporter activity
A0015768biological_processmaltose transport
A0016020cellular_componentmembrane
A0030163biological_processprotein catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0032354biological_processresponse to follicle-stimulating hormone
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
A0071548biological_processresponse to dexamethasone
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
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0008643biological_processcarbohydrate transport
B0015144molecular_functioncarbohydrate transmembrane transporter activity
B0015768biological_processmaltose transport
B0016020cellular_componentmembrane
B0030163biological_processprotein catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0032354biological_processresponse to follicle-stimulating hormone
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
B0071548biological_processresponse to dexamethasone
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 Residues2
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
CSER250
CSER251

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
CTHR254
AHIS486
AHIS492
BHIS482
BHIS486
BHIS492

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CASN73
AASN745
AASN1142
AASN1385
BASN310
BASN745
BASN1142
BASN1385

site_idSWS_FT_FI4
Number of Residues20
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12421832
ChainResidueDetails
AASN322
AASN1439
BASN322
BASN349
BASN400
BASN521
BASN539
BASN645
BASN946
BASN1146
BASN1243
AASN349
BASN1439
AASN400
AASN521
AASN539
AASN645
AASN946
AASN1146
AASN1243

227111

PDB entries from 2024-11-06

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