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6JZC

Structural basis of tubulin detyrosination

Functional Information from GO Data
ChainGOidnamespacecontents
A0000768biological_processsyncytium formation by plasma membrane fusion
A0001938biological_processpositive regulation of endothelial cell proliferation
A0003779molecular_functionactin binding
A0004180molecular_functioncarboxypeptidase activity
A0004181molecular_functionmetallocarboxypeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0006508biological_processproteolysis
A0008017molecular_functionmicrotubule binding
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0045765biological_processregulation of angiogenesis
A0045766biological_processpositive regulation of angiogenesis
A0060674biological_processplacenta blood vessel development
A0060711biological_processlabyrinthine layer development
A0060716biological_processlabyrinthine layer blood vessel development
A0061564biological_processaxon development
A0106423molecular_functiontubulin-tyrosine carboxypeptidase
A0140253biological_processcell-cell fusion
B0000768biological_processsyncytium formation by plasma membrane fusion
B0001938biological_processpositive regulation of endothelial cell proliferation
B0003779molecular_functionactin binding
B0004180molecular_functioncarboxypeptidase activity
B0004181molecular_functionmetallocarboxypeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0006508biological_processproteolysis
B0008017molecular_functionmicrotubule binding
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0045765biological_processregulation of angiogenesis
B0045766biological_processpositive regulation of angiogenesis
B0060674biological_processplacenta blood vessel development
B0060711biological_processlabyrinthine layer development
B0060716biological_processlabyrinthine layer blood vessel development
B0061564biological_processaxon development
B0106423molecular_functiontubulin-tyrosine carboxypeptidase
B0140253biological_processcell-cell fusion
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0006508biological_processproteolysis
C0008017molecular_functionmicrotubule binding
C0009306biological_processprotein secretion
C0010596biological_processnegative regulation of endothelial cell migration
C0016504molecular_functionpeptidase activator activity
C0031397biological_processnegative regulation of protein ubiquitination
C0045177cellular_componentapical part of cell
C0061564biological_processaxon development
C1905048biological_processregulation of metallopeptidase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0006508biological_processproteolysis
D0008017molecular_functionmicrotubule binding
D0009306biological_processprotein secretion
D0010596biological_processnegative regulation of endothelial cell migration
D0016504molecular_functionpeptidase activator activity
D0031397biological_processnegative regulation of protein ubiquitination
D0045177cellular_componentapical part of cell
D0061564biological_processaxon development
D1905048biological_processregulation of metallopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GOL A 401
ChainResidue
ALEU111
AGLN112
ASER206
AASP217
ALYS218
APRO219

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 402
ChainResidue
AALA213
AMET216
AHOH511
AHOH525
AHOH542
ALYS119
ASER210
AARG211

site_idAC3
Number of Residues10
Detailsbinding site for residue GOL A 403
ChainResidue
AASN52
ALYS53
ASER54
AGLY55
APHE130
APHE131
AGLU132
AGLU148
AHOH513
AHOH558

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 404
ChainResidue
ATRP63
AARG85
AASN86
AHOH569
DGLU38

site_idAC5
Number of Residues8
Detailsbinding site for residue GOL B 401
ChainResidue
BGLN112
BSER206
BLEU207
BASP217
BLYS218
BPRO219
BHOH559
BHOH575

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL B 402
ChainResidue
BSER210
BARG211
BALA213
BMET216
BHOH516
BHOH531
BHOH542

site_idAC7
Number of Residues10
Detailsbinding site for residue GOL B 403
ChainResidue
BASN52
BLYS53
BSER54
BGLY55
BPHE56
BPHE130
BPHE131
BGLU132
BGLU148
BHOH543

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL B 404
ChainResidue
BTRP63
BARG85
BHOH532
CLEU31
CGLU38

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:29146868, ECO:0000305|PubMed:26794318
ChainResidueDetails
ACYS158
BCYS158

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:26794318
ChainResidueDetails
AHIS193
ASER210
BHIS193
BSER210

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q86V25
ChainResidueDetails
ASER302
BSER302

218853

PDB entries from 2024-04-24

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