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8B0H

2C9, C5b9-CD59 cryoEM structure

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006954biological_processinflammatory response
A0006956biological_processcomplement activation
B0005579cellular_componentmembrane attack complex
B0006955biological_processimmune response
C0005579cellular_componentmembrane attack complex
C0006955biological_processimmune response
D0005579cellular_componentmembrane attack complex
D0006955biological_processimmune response
E0005579cellular_componentmembrane attack complex
E0006955biological_processimmune response
F0005579cellular_componentmembrane attack complex
F0006956biological_processcomplement activation
H0005579cellular_componentmembrane attack complex
H0006955biological_processimmune response
I0005579cellular_componentmembrane attack complex
I0006955biological_processimmune response
Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. NFDaqQFAGTWLLV
ChainResidueDetails
FASN21-VAL34

site_idPS01177
Number of Residues35
DetailsANAPHYLATOXIN_1 Anaphylatoxin domain signature. CCydGacvnnde.TCEqraarisl.GprCikafte.CC
ChainResidueDetails
ACYS698-CYS732

site_idPS00983
Number of Residues44
DetailsLY6_UPAR Ly-6 / u-PAR domain signature. QCYnCpnptad..Cktav....NCSsdfdaClitkaglqvynkcwkfeh......C
ChainResidueDetails
GGLN2-CYS45

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. ChCkpYtfGAaC
ChainResidueDetails
ECYS487-CYS498
CCYS475-CYS486
HCYS507-CYS518
BCYS541-CYS552
DCYS469-CYS480

site_idPS00279
Number of Residues12
DetailsMACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YrrlidqYGTHY
ChainResidueDetails
ETYR300-TYR311
CTYR292-TYR303
HTYR314-TYR325
BTYR354-TYR365
DTYR279-TYR290

site_idPS01186
Number of Residues16
DetailsEGF_2 EGF-like domain signature 2. CvCkmPYecgpsldvC
ChainResidueDetails
CCYS713-CYS728
HCYS505-CYS518

site_idPS01209
Number of Residues24
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIskslv.CNgdsDCdedsADEdr...C
ChainResidueDetails
ECYS78-CYS100
CCYS96-CYS119
HCYS91-CYS113
BCYS151-CYS173
DCYS79-CYS101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues70
DetailsTRANSMEM: Beta stranded => ECO:0000255
ChainResidueDetails
HVAL293-TYR309
HTYR314-GLY333
IVAL293-TYR309
ITYR314-GLY333

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by thrombin
ChainResidueDetails
HHIS244
IHIS244
BTRP568
BTRP571
BTRP574

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839
ChainResidueDetails
HTRP27
ITRP27
CTRP509

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839
ChainResidueDetails
HTRP30
ITRP30

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801
ChainResidueDetails
HASN256
IASN256

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801
ChainResidueDetails
HASN394
IASN394

221051

PDB entries from 2024-06-12

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