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

9BP6

Structure of alpha1B and betaI/IVb microtubule bound to GMPCPP

Replaces:  8V2I
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0003725molecular_functiondouble-stranded RNA binding
A0003924molecular_functionGTPase activity
A0005198molecular_functionstructural molecule activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0005881cellular_componentcytoplasmic microtubule
A0005929cellular_componentcilium
A0007017biological_processmicrotubule-based process
A0015630cellular_componentmicrotubule cytoskeleton
A0016787molecular_functionhydrolase activity
A0030182biological_processneuron differentiation
A0030705biological_processcytoskeleton-dependent intracellular transport
A0031625molecular_functionubiquitin protein ligase binding
A0051301biological_processcell division
B0000166molecular_functionnucleotide binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0003924molecular_functionGTPase activity
B0005198molecular_functionstructural molecule activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005641cellular_componentnuclear envelope lumen
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0005929cellular_componentcilium
B0007017biological_processmicrotubule-based process
B0015630cellular_componentmicrotubule cytoskeleton
B0019904molecular_functionprotein domain specific binding
B0030705biological_processcytoskeleton-dependent intracellular transport
B0031625molecular_functionubiquitin protein ligase binding
B0032794molecular_functionGTPase activating protein binding
B0032991cellular_componentprotein-containing complex
B0035578cellular_componentazurophil granule lumen
B0036464cellular_componentcytoplasmic ribonucleoprotein granule
B0042267biological_processnatural killer cell mediated cytotoxicity
B0042288molecular_functionMHC class I protein binding
B0044297cellular_componentcell body
B0044877molecular_functionprotein-containing complex binding
B0045121cellular_componentmembrane raft
B0045171cellular_componentintercellular bridge
B0046872molecular_functionmetal ion binding
B0050807biological_processregulation of synapse organization
B0051301biological_processcell division
B0070062cellular_componentextracellular exosome
B0071895biological_processodontoblast differentiation
B0072686cellular_componentmitotic spindle
B0097228cellular_componentsperm principal piece
B0097229cellular_componentsperm end piece
B0097542cellular_componentciliary tip
I0000166molecular_functionnucleotide binding
I0000226biological_processmicrotubule cytoskeleton organization
I0000278biological_processmitotic cell cycle
I0003725molecular_functiondouble-stranded RNA binding
I0003924molecular_functionGTPase activity
I0005198molecular_functionstructural molecule activity
I0005200molecular_functionstructural constituent of cytoskeleton
I0005515molecular_functionprotein binding
I0005525molecular_functionGTP binding
I0005737cellular_componentcytoplasm
I0005856cellular_componentcytoskeleton
I0005874cellular_componentmicrotubule
I0005881cellular_componentcytoplasmic microtubule
I0005929cellular_componentcilium
I0007017biological_processmicrotubule-based process
I0015630cellular_componentmicrotubule cytoskeleton
I0016787molecular_functionhydrolase activity
I0030182biological_processneuron differentiation
I0030705biological_processcytoskeleton-dependent intracellular transport
I0031625molecular_functionubiquitin protein ligase binding
I0051301biological_processcell division
Q0000166molecular_functionnucleotide binding
Q0000226biological_processmicrotubule cytoskeleton organization
Q0000278biological_processmitotic cell cycle
Q0003924molecular_functionGTPase activity
Q0005198molecular_functionstructural molecule activity
Q0005200molecular_functionstructural constituent of cytoskeleton
Q0005515molecular_functionprotein binding
Q0005525molecular_functionGTP binding
Q0005576cellular_componentextracellular region
Q0005634cellular_componentnucleus
Q0005641cellular_componentnuclear envelope lumen
Q0005737cellular_componentcytoplasm
Q0005829cellular_componentcytosol
Q0005856cellular_componentcytoskeleton
Q0005874cellular_componentmicrotubule
Q0005929cellular_componentcilium
Q0007017biological_processmicrotubule-based process
Q0015630cellular_componentmicrotubule cytoskeleton
Q0019904molecular_functionprotein domain specific binding
Q0030705biological_processcytoskeleton-dependent intracellular transport
Q0031625molecular_functionubiquitin protein ligase binding
Q0032794molecular_functionGTPase activating protein binding
Q0032991cellular_componentprotein-containing complex
Q0035578cellular_componentazurophil granule lumen
Q0036464cellular_componentcytoplasmic ribonucleoprotein granule
Q0042267biological_processnatural killer cell mediated cytotoxicity
Q0042288molecular_functionMHC class I protein binding
Q0044297cellular_componentcell body
Q0044877molecular_functionprotein-containing complex binding
Q0045121cellular_componentmembrane raft
Q0045171cellular_componentintercellular bridge
Q0046872molecular_functionmetal ion binding
Q0050807biological_processregulation of synapse organization
Q0051301biological_processcell division
Q0070062cellular_componentextracellular exosome
Q0071895biological_processodontoblast differentiation
Q0072686cellular_componentmitotic spindle
Q0097228cellular_componentsperm principal piece
Q0097229cellular_componentsperm end piece
Q0097542cellular_componentciliary tip
Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
AGLY142-GLY148
BGLY140-GLY146
site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
BMET1-ILE4
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsMotif: {"description":"MREC motif","evidences":[{"source":"PubMed","id":"31727855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"34996871","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38609661","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8VT7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34996871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35482892","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38609661","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7SJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7Z6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8VT7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues10
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues6
DetailsMotif: {"description":"MREI motif","evidences":[{"source":"PubMed","id":"31727855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues6
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"PubMed","id":"16371510","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Campbell A.","Ozanne B.W.","Lourenco F.","Olson M.F."]}}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon