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3HRZ

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
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
D0008236molecular_functionserine-type peptidase activity
D0009617biological_processresponse to bacterium
D0070062cellular_componentextracellular exosome
D0072562cellular_componentblood microparticle
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 Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
DHIS501
DASP551
DSER674
AASP520

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754
ChainResidueDetails
DASN97
DASP260

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754
ChainResidueDetails
DASN117

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:2006911
ChainResidueDetails
DLYS266

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754
ChainResidueDetails
DASN353

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DSER674
DASP551
DHIS501

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DGLY675
DSER674
DASP551
DHIS501

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DSER674
DASP551
DGLY672
DHIS501

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP551
DHIS501

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DSER674
DGLY672

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DGLY675
DSER674

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PDB entries from 2024-07-24

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