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4ABO

Mal3 CH domain homology model and mammalian tubulin (2XRP) docked into the 8.6-Angstrom cryo-EM map of Mal3-GTPgammaS-microtubules

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0001764biological_processneuron migration
A0003924molecular_functionGTPase activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0007017biological_processmicrotubule-based process
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0005200molecular_functionstructural constituent of cytoskeleton
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0016787molecular_functionhydrolase activity
B0030182biological_processneuron differentiation
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000226biological_processmicrotubule cytoskeleton organization
C0000278biological_processmitotic cell cycle
C0001764biological_processneuron migration
C0003924molecular_functionGTPase activity
C0005200molecular_functionstructural constituent of cytoskeleton
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0007017biological_processmicrotubule-based process
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0000226biological_processmicrotubule cytoskeleton organization
D0000278biological_processmitotic cell cycle
D0005200molecular_functionstructural constituent of cytoskeleton
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005874cellular_componentmicrotubule
D0007017biological_processmicrotubule-based process
D0016787molecular_functionhydrolase activity
D0030182biological_processneuron differentiation
D0046872molecular_functionmetal ion binding
E0000166molecular_functionnucleotide binding
E0000226biological_processmicrotubule cytoskeleton organization
E0000278biological_processmitotic cell cycle
E0001764biological_processneuron migration
E0003924molecular_functionGTPase activity
E0005200molecular_functionstructural constituent of cytoskeleton
E0005515molecular_functionprotein binding
E0005525molecular_functionGTP binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005874cellular_componentmicrotubule
E0007017biological_processmicrotubule-based process
E0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0000226biological_processmicrotubule cytoskeleton organization
F0000278biological_processmitotic cell cycle
F0005200molecular_functionstructural constituent of cytoskeleton
F0005525molecular_functionGTP binding
F0005737cellular_componentcytoplasm
F0005856cellular_componentcytoskeleton
F0005874cellular_componentmicrotubule
F0007017biological_processmicrotubule-based process
F0016787molecular_functionhydrolase activity
F0030182biological_processneuron differentiation
F0046872molecular_functionmetal ion binding
G0000166molecular_functionnucleotide binding
G0000226biological_processmicrotubule cytoskeleton organization
G0000278biological_processmitotic cell cycle
G0001764biological_processneuron migration
G0003924molecular_functionGTPase activity
G0005200molecular_functionstructural constituent of cytoskeleton
G0005515molecular_functionprotein binding
G0005525molecular_functionGTP binding
G0005737cellular_componentcytoplasm
G0005856cellular_componentcytoskeleton
G0005874cellular_componentmicrotubule
G0007017biological_processmicrotubule-based process
G0046872molecular_functionmetal ion binding
H0000166molecular_functionnucleotide binding
H0000226biological_processmicrotubule cytoskeleton organization
H0000278biological_processmitotic cell cycle
H0005200molecular_functionstructural constituent of cytoskeleton
H0005525molecular_functionGTP binding
H0005737cellular_componentcytoplasm
H0005856cellular_componentcytoskeleton
H0005874cellular_componentmicrotubule
H0007017biological_processmicrotubule-based process
H0016787molecular_functionhydrolase activity
H0030182biological_processneuron differentiation
H0046872molecular_functionmetal ion binding
I0008017molecular_functionmicrotubule binding
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GSP C 1438
ChainResidue
BGLU254
CSER140
CGLY142
CGLY144
CTHR145
CGLY146
CASP179
CGLU183
CASN206
CTYR224
CASN228
CGLY10
CGLN11
CCYS12
CGLN15
CGLU71
CALA99
CGLY100
CASN101

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GSP A 1438
ChainResidue
AGLY10
AGLN11
ACYS12
AGLN15
AGLU71
AALA99
AGLY100
AASN101
ASER140
AGLY142
AGLY144
ATHR145
AGLY146
AASP179
AGLU183
AASN206
ATYR224
AASN228

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GTP B 500
ChainResidue
ALEU248
ALYS254
BGLY10
BGLN11
BALA12
BGLN15
BALA99
BALA100
BASN101
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BILE171
BGLU183
BASN206
BTYR224
BASN228

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GSP E 1438
ChainResidue
EGLY10
EGLN11
ECYS12
EGLN15
EGLU71
EALA99
EGLY100
EASN101
ESER140
EGLY142
EGLY144
ETHR145
EGLY146
EASP179
EGLU183
EASN206
ETYR224
EASN228

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GTP D 500
ChainResidue
CLEU248
CLYS254
DGLY10
DGLN11
DALA12
DGLN15
DALA99
DALA100
DASN101
DSER140
DGLY143
DGLY144
DTHR145
DGLY146
DILE171
DGLU183
DASN206
DTYR224
DASN228

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GTP F 500
ChainResidue
FALA99
FALA100
FASN101
FSER140
FGLY143
FGLY144
FTHR145
FGLY146
FILE171
FGLU183
FASN206
FTYR224
FASN228
ELEU248
ELYS254
FGLY10
FGLN11
FALA12
FGLN15

site_idAC7
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GTP H 500
ChainResidue
GLEU248
HGLY10
HGLN11
HALA12
HGLN15
HALA99
HALA100
HASN101
HSER140
HGLY143
HGLY144
HTHR145
HGLY146
HILE171
HGLU183
HASN206
HTYR224
HASN228

site_idAC8
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GSP G 1438
ChainResidue
FGLU254
GGLY10
GGLN11
GCYS12
GGLN15
GGLU71
GALA99
GGLY100
GASN101
GSER140
GGLY142
GGLY144
GTHR145
GGLY146
GASP179
GGLU183
GASN206
GTYR224
GASN228

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
AGLY142-GLY148
BGLY142-GLY148

site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
AMET1-ILE4

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues72
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"UniProtKB","id":"Q13885","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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