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5JPM

Structure of the complex of human complement C4 with MASP-2 rebuilt using iMDFF

Replaces:  4FXG
Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
B0004866molecular_functionendopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006954biological_processinflammatory response
B0006956biological_processcomplement activation
C0005576cellular_componentextracellular region
D0004866molecular_functionendopeptidase inhibitor activity
E0004866molecular_functionendopeptidase inhibitor activity
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0006954biological_processinflammatory response
E0006956biological_processcomplement activation
F0005576cellular_componentextracellular region
H0004252molecular_functionserine-type endopeptidase activity
H0006508biological_processproteolysis
J0004252molecular_functionserine-type endopeptidase activity
J0006508biological_processproteolysis
Functional Information from PROSITE/UniProt
site_idPS00477
Number of Residues9
DetailsALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PrGCGEQtM
ChainResidueDetails
BPRO1007-MET1015

site_idPS01177
Number of Residues35
DetailsANAPHYLATOXIN_1 Anaphylatoxin domain signature. CCqdGvtrlpmmrSCEqraarvq..QpdCrepfls.CC
ChainResidueDetails
BCYS702-CYS736

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system
ChainResidueDetails
HHIS483
HASP532
HALA633
JHIS483
JASP532
JALA633

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
BSER918
ESER918

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Sulfotyrosine => ECO:0000269|PubMed:3944109
ChainResidueDetails
BTYS1417
BTYS1420
BTYR1422
ETYS1417
ETYS1420
ETYR1422

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
BASN862
EASN862

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:23234360
ChainResidueDetails
BTHR1244
ETHR1244

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218
ChainResidueDetails
BASN1328
EASN1328

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
BASN1391
EASN1391

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Isoglutamyl cysteine thioester (Cys-Gln)
ChainResidueDetails
BCYS1010
BGLN1013
ECYS1010
EGLN1013

226707

PDB entries from 2024-10-30

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