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7Y5N

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0006955biological_processimmune response
C0004175molecular_functionendopeptidase activity
C0004222molecular_functionmetalloendopeptidase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0006508biological_processproteolysis
C0007166biological_processcell surface receptor signaling pathway
C0007565biological_processfemale pregnancy
C0008237molecular_functionmetallopeptidase activity
C0008270molecular_functionzinc ion binding
C0019538biological_processprotein metabolic process
C0030163biological_processprotein catabolic process
C0032354biological_processresponse to follicle-stimulating hormone
C0046872molecular_functionmetal ion binding
C0071548biological_processresponse to dexamethasone
D0004175molecular_functionendopeptidase activity
D0004222molecular_functionmetalloendopeptidase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0006508biological_processproteolysis
D0007166biological_processcell surface receptor signaling pathway
D0007565biological_processfemale pregnancy
D0008237molecular_functionmetallopeptidase activity
D0008270molecular_functionzinc ion binding
D0019538biological_processprotein metabolic process
D0030163biological_processprotein catabolic process
D0032354biological_processresponse to follicle-stimulating hormone
D0046872molecular_functionmetal ion binding
D0071548biological_processresponse to dexamethasone
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TMIHEIGHSL
ChainResidueDetails
CTHR479-LEU488

site_idPS00615
Number of Residues24
DetailsC_TYPE_LECTIN_1 C-type lectin domain signature. CValctrggh....WRRAHClrrlp.FIC
ChainResidueDetails
ACYS197-CYS220

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
CGLU483
DGLU483

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
CHIS482
CHIS486
CHIS492
DHIS482
DHIS486
DHIS492

site_idSWS_FT_FI3
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CASN310
CASN745
CASN1142
CASN1385
DASN310
DASN745
DASN1142
DASN1385

site_idSWS_FT_FI4
Number of Residues20
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12421832
ChainResidueDetails
CASN322
CASN1439
DASN322
DASN349
DASN400
DASN521
DASN539
DASN645
DASN946
DASN1146
DASN1243
CASN349
DASN1439
CASN400
CASN521
CASN539
CASN645
CASN946
CASN1146
CASN1243

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:7524900, ECO:0000269|PubMed:8507662
ChainResidueDetails
AASN86

222036

PDB entries from 2024-07-03

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