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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
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
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
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
B0046872molecular_functionmetal ion binding
C0000226biological_processmicrotubule cytoskeleton organization
C0000278biological_processmitotic cell cycle
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
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
D0046872molecular_functionmetal ion binding
E0000226biological_processmicrotubule cytoskeleton organization
E0000278biological_processmitotic cell cycle
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
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
F0046872molecular_functionmetal ion binding
G0000226biological_processmicrotubule cytoskeleton organization
G0000278biological_processmitotic cell cycle
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
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
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 Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
BGLU254
CGLY144
CTHR145
CGLY146
CASN206
CASN228
EGLN11
ESER140
EGLY144
ETHR145
EGLY146
DGLU254
EASN206
EASN228
GGLN11
GSER140
GGLY144
GTHR145
GGLY146
GASN206
GASN228
FGLU254
HGLU254
AGLY146
AASN206
AASN228
CGLN11
CSER140

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
BGLN11
DGLU71
DSER140
DGLY144
DTHR145
DTHR179
DASN206
DASN228
FGLN11
FGLU71
FSER140
BGLU71
FGLY144
FTHR145
FTHR179
FASN206
FASN228
HGLN11
HGLU71
HSER140
HGLY144
HTHR145
BSER140
HTHR179
HASN206
HASN228
BGLY144
BTHR145
BTHR179
BASN206
BASN228
DGLN11

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Involved in polymerization
ChainResidueDetails
BTYR451
DTYR451
FTYR451
HTYR451

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q71U36
ChainResidueDetails
BLYS40
DLYS40
FLYS40
HLYS40

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P68373
ChainResidueDetails
BTYR282
DTYR282
FTYR282
HTYR282

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68373
ChainResidueDetails
BSER439
DSER439
FSER439
HSER439
ETHR287
ETHR292
GTHR287
GTHR292

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q71U36
ChainResidueDetails
BGLU443
DGLU443
FGLU443
HGLU443

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:P68369
ChainResidueDetails
BGLU445
DGLU445
FGLU445
HGLU445

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q71U36
ChainResidueDetails
BTYR451
DTYR451
FTYR451
HTYR451

site_idSWS_FT_FI10
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
ALYS326
CLYS326
ELYS326
GLYS326

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PDB entries from 2024-07-10

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