Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5O32

The structure of complement complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
B0004866molecular_functionendopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
D0016020cellular_componentmembrane
E0004866molecular_functionendopeptidase inhibitor activity
F0004866molecular_functionendopeptidase inhibitor activity
F0005576cellular_componentextracellular region
F0005615cellular_componentextracellular space
H0016020cellular_componentmembrane
I0004252molecular_functionserine-type endopeptidase activity
I0006508biological_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. PsGCGEQnM
ChainResidueDetails
BPRO1007-MET1015

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ILEU376-CYS381

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAckGDSGGPLV
ChainResidueDetails
IASP519-VAL530

site_idPS01209
Number of Residues23
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIpsqyq.CNgevDCitg.EDEvg...C
ChainResidueDetails
DCYS271-CYS293

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000250|UniProtKB:P00750
ChainResidueDetails
IHIS380
DASP283
DASP289
DGLU290
HLYS239
HASP242
HILE244
HASP246
HASP252
HGLU253
HTYR276
IASP429
HASN279
HGLU281
HASP283
HASP289
HGLU290
ISER525
JHIS380
JASP429
JSER525
DTYR276
DASN279
DGLU281

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC
ChainResidueDetails
IASN464
JASN464
HASN70
HASN177
ESER38
ESER70
ESER297
ESER303

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC
ChainResidueDetails
IASN494
JASN494

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC
ChainResidueDetails
IASN536
JASN536
BSER1573
FSER968
FSER1321
FSER1573

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17051150
ChainResidueDetails
BASN939
FASN939

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
BASN1617
FASN1617

site_idSWS_FT_FI7
Number of Residues4
DetailsCROSSLNK: Isoglutamyl cysteine thioester (Cys-Gln)
ChainResidueDetails
BCYS1010
BGLN1013
FCYS1010
FGLN1013

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon