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6NVQ

Crystal structure of the VASH1-SVBP complex

Functional Information from GO Data
ChainGOidnamespacecontents
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0006508biological_processproteolysis
B0008017molecular_functionmicrotubule binding
B0009306biological_processprotein secretion
B0010596biological_processnegative regulation of endothelial cell migration
B0016504molecular_functionpeptidase activator activity
B0031397biological_processnegative regulation of protein ubiquitination
B0045177cellular_componentapical part of cell
B0061564biological_processaxon development
B1905048biological_processregulation of metallopeptidase activity
C0005737cellular_componentcytoplasm
C0045765biological_processregulation of angiogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue GOL C 401
ChainResidue
CTHR185
CASN210
CALA212

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL C 402
ChainResidue
CVAL109
CGLN113
CTHR161
CLYS162

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:29146869, ECO:0000305|PubMed:26794318
ChainResidueDetails
CALA169

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:26794318
ChainResidueDetails
CHIS204
CSER221

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage => ECO:0000305|PubMed:16488400
ChainResidueDetails
CARG29
CARG76

219140

PDB entries from 2024-05-01

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