Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3HS0

Cobra Venom Factor (CVF) in complex with human factor B

Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
B0004866molecular_functionendopeptidase inhibitor activity
C0005576cellular_componentextracellular region
D0001848molecular_functioncomplement binding
D0002376biological_processimmune system process
D0004252molecular_functionserine-type endopeptidase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005886cellular_componentplasma membrane
D0006508biological_processproteolysis
D0006956biological_processcomplement activation
D0006957biological_processcomplement activation, alternative pathway
D0008233molecular_functionpeptidase activity
D0008236molecular_functionserine-type peptidase activity
D0009617biological_processresponse to bacterium
D0009986cellular_componentcell surface
D0016787molecular_functionhydrolase activity
D0045087biological_processinnate immune response
D0070062cellular_componentextracellular exosome
D0072562cellular_componentblood microparticle
D0106139cellular_componentsymbiont cell surface
F0004866molecular_functionendopeptidase inhibitor activity
G0004866molecular_functionendopeptidase inhibitor activity
H0005576cellular_componentextracellular region
I0001848molecular_functioncomplement binding
I0002376biological_processimmune system process
I0004252molecular_functionserine-type endopeptidase activity
I0005515molecular_functionprotein binding
I0005576cellular_componentextracellular region
I0005615cellular_componentextracellular space
I0005886cellular_componentplasma membrane
I0006508biological_processproteolysis
I0006956biological_processcomplement activation
I0006957biological_processcomplement activation, alternative pathway
I0008233molecular_functionpeptidase activity
I0008236molecular_functionserine-type peptidase activity
I0009617biological_processresponse to bacterium
I0009986cellular_componentcell surface
I0016787molecular_functionhydrolase activity
I0045087biological_processinnate immune response
I0070062cellular_componentextracellular exosome
I0072562cellular_componentblood microparticle
I0106139cellular_componentsymbiont cell surface
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DDNEDGFIAdsDI
ChainResidueDetails
BASP711-ILE723
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
DLEU497-CYS502
site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. NTcrGDSGGPLI
ChainResidueDetails
DASN668-ILE679
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19574954","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21217642","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues286
DetailsDomain: {"description":"NTR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00295","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues118
DetailsDomain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues114
DetailsDomain: {"description":"Sushi 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues199
DetailsDomain: {"description":"VWFA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00219","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"10637221","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15016353","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q0P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsSite: {"description":"Cleavage; by CFD","evidences":[{"source":"PubMed","id":"6769474","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17310251","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6546754","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17310251","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19574954","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6546754","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"2006911","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17310251","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19503103","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19574954","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6546754","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WIN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DSER674
DASP551
DHIS501
site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ISER674
IGLY672
site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DGLY675
DSER674
site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
IGLY675
ISER674
site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ISER674
IASP551
IHIS501
site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DGLY675
DSER674
DASP551
DHIS501
site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
IGLY675
ISER674
IASP551
IHIS501
site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DSER674
DASP551
DGLY672
DHIS501
site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ISER674
IASP551
IGLY672
IHIS501
site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP551
DHIS501
site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
IASP551
IHIS501
site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DSER674
DGLY672

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon