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6J4V

Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0045765biological_processregulation of angiogenesis
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
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue PO4 A 301
ChainResidue
AARG102
ASER104
AHOH432

site_idAC2
Number of Residues4
Detailsbinding site for residue PO4 A 302
ChainResidue
ALYS183
AHIS192
ALYS245
ALYS247

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 303
ChainResidue
AASN86
AHOH405
BGLU38
ATRP63
AARG85

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL A 304
ChainResidue
ALYS119
ASER210
AARG211
AARG212
AALA213
AMET216
AHOH470
AHOH541

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 305
ChainResidue
APRO93
ASER94
APRO96
ATHR120
AHOH475
BTYR40

site_idAC6
Number of Residues3
Detailsbinding site for residue GOL A 306
ChainResidue
APRO99
AASN100
AHOH426

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Involved in polymerization
ChainResidueDetails
CTYR451

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68373
ChainResidueDetails
ASER210
CSER439

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000269|PubMed:32747782
ChainResidueDetails
CGLU443

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:P68369
ChainResidueDetails
CGLU445

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000269|PubMed:10339593
ChainResidueDetails
CTYR451

221051

PDB entries from 2024-06-12

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