Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6EVX

Cryo-EM structure of GDP.Pi-microtubule rapidly co-polymerised with doublecortin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000226	biological_process	microtubule cytoskeleton organization
A	0000278	biological_process	mitotic cell cycle
A	0003924	molecular_function	GTPase activity
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0005874	cellular_component	microtubule
A	0007017	biological_process	microtubule-based process
A	0015630	cellular_component	microtubule cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
B	0000226	biological_process	microtubule cytoskeleton organization
B	0000278	biological_process	mitotic cell cycle
B	0003924	molecular_function	GTPase activity
B	0005200	molecular_function	structural constituent of cytoskeleton
B	0005515	molecular_function	protein binding
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0005874	cellular_component	microtubule
B	0007017	biological_process	microtubule-based process
B	0046872	molecular_function	metal ion binding
C	0000226	biological_process	microtubule cytoskeleton organization
C	0000278	biological_process	mitotic cell cycle
C	0003924	molecular_function	GTPase activity
C	0005200	molecular_function	structural constituent of cytoskeleton
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0005856	cellular_component	cytoskeleton
C	0005874	cellular_component	microtubule
C	0007017	biological_process	microtubule-based process
C	0015630	cellular_component	microtubule cytoskeleton
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
D	0000226	biological_process	microtubule cytoskeleton organization
D	0000278	biological_process	mitotic cell cycle
D	0003924	molecular_function	GTPase activity
D	0005200	molecular_function	structural constituent of cytoskeleton
D	0005515	molecular_function	protein binding
D	0005525	molecular_function	GTP binding
D	0005737	cellular_component	cytoplasm
D	0005856	cellular_component	cytoskeleton
D	0005874	cellular_component	microtubule
D	0007017	biological_process	microtubule-based process
D	0046872	molecular_function	metal ion binding
E	0000226	biological_process	microtubule cytoskeleton organization
E	0000278	biological_process	mitotic cell cycle
E	0003924	molecular_function	GTPase activity
E	0005200	molecular_function	structural constituent of cytoskeleton
E	0005525	molecular_function	GTP binding
E	0005737	cellular_component	cytoplasm
E	0005856	cellular_component	cytoskeleton
E	0005874	cellular_component	microtubule
E	0007017	biological_process	microtubule-based process
E	0015630	cellular_component	microtubule cytoskeleton
E	0016787	molecular_function	hydrolase activity
E	0046872	molecular_function	metal ion binding
F	0000226	biological_process	microtubule cytoskeleton organization
F	0000278	biological_process	mitotic cell cycle
F	0003924	molecular_function	GTPase activity
F	0005200	molecular_function	structural constituent of cytoskeleton
F	0005515	molecular_function	protein binding
F	0005525	molecular_function	GTP binding
F	0005737	cellular_component	cytoplasm
F	0005856	cellular_component	cytoskeleton
F	0005874	cellular_component	microtubule
F	0007017	biological_process	microtubule-based process
F	0046872	molecular_function	metal ion binding
G	0000226	biological_process	microtubule cytoskeleton organization
G	0000278	biological_process	mitotic cell cycle
G	0003924	molecular_function	GTPase activity
G	0005200	molecular_function	structural constituent of cytoskeleton
G	0005515	molecular_function	protein binding
G	0005525	molecular_function	GTP binding
G	0005737	cellular_component	cytoplasm
G	0005856	cellular_component	cytoskeleton
G	0005874	cellular_component	microtubule
G	0007017	biological_process	microtubule-based process
G	0046872	molecular_function	metal ion binding
H	0000226	biological_process	microtubule cytoskeleton organization
H	0000278	biological_process	mitotic cell cycle
H	0003924	molecular_function	GTPase activity
H	0005200	molecular_function	structural constituent of cytoskeleton
H	0005515	molecular_function	protein binding
H	0005525	molecular_function	GTP binding
H	0005737	cellular_component	cytoplasm
H	0005856	cellular_component	cytoskeleton
H	0005874	cellular_component	microtubule
H	0007017	biological_process	microtubule-based process
H	0046872	molecular_function	metal ion binding
I	0000226	biological_process	microtubule cytoskeleton organization
I	0000278	biological_process	mitotic cell cycle
I	0003924	molecular_function	GTPase activity
I	0005200	molecular_function	structural constituent of cytoskeleton
I	0005515	molecular_function	protein binding
I	0005525	molecular_function	GTP binding
I	0005737	cellular_component	cytoplasm
I	0005856	cellular_component	cytoskeleton
I	0005874	cellular_component	microtubule
I	0007017	biological_process	microtubule-based process
I	0046872	molecular_function	metal ion binding
J	0000226	biological_process	microtubule cytoskeleton organization
J	0000278	biological_process	mitotic cell cycle
J	0003924	molecular_function	GTPase activity
J	0005200	molecular_function	structural constituent of cytoskeleton
J	0005525	molecular_function	GTP binding
J	0005737	cellular_component	cytoplasm
J	0005856	cellular_component	cytoskeleton
J	0005874	cellular_component	microtubule
J	0007017	biological_process	microtubule-based process
J	0015630	cellular_component	microtubule cytoskeleton
J	0016787	molecular_function	hydrolase activity
J	0046872	molecular_function	metal ion binding
K	0000226	biological_process	microtubule cytoskeleton organization
K	0000278	biological_process	mitotic cell cycle
K	0003924	molecular_function	GTPase activity
K	0005200	molecular_function	structural constituent of cytoskeleton
K	0005525	molecular_function	GTP binding
K	0005737	cellular_component	cytoplasm
K	0005856	cellular_component	cytoskeleton
K	0005874	cellular_component	microtubule
K	0007017	biological_process	microtubule-based process
K	0015630	cellular_component	microtubule cytoskeleton
K	0016787	molecular_function	hydrolase activity
K	0046872	molecular_function	metal ion binding
L	0000226	biological_process	microtubule cytoskeleton organization
L	0000278	biological_process	mitotic cell cycle
L	0003924	molecular_function	GTPase activity
L	0005200	molecular_function	structural constituent of cytoskeleton
L	0005525	molecular_function	GTP binding
L	0005737	cellular_component	cytoplasm
L	0005856	cellular_component	cytoskeleton
L	0005874	cellular_component	microtubule
L	0007017	biological_process	microtubule-based process
L	0015630	cellular_component	microtubule cytoskeleton
L	0016787	molecular_function	hydrolase activity
L	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue GDP F 501

Chain	Residue
E	PO4501
F	ASP177
F	ASN204
F	TYR222
F	ASN226
F	GLY10
F	GLN11
F	CYS12
F	SER138
F	GLY141
F	GLY142
F	THR143
F	GLY144

site_id	AC2
Number of Residues	18
Details	binding site for residue GTP A 501

Chain	Residue
A	GLY10
A	GLN11
A	ALA12
A	GLN15
A	GLU71
A	ALA99
A	ALA100
A	ASN101
A	SER140
A	GLY143
A	GLY144
A	THR145
A	GLY146
A	ASN206
A	TYR224
A	ASN228
A	ILE231
A	MG502

site_id	AC3
Number of Residues	3
Details	binding site for residue MG A 502

Chain	Residue
A	GLN11
A	GLU71
A	GTP501

site_id	AC4
Number of Residues	6
Details	binding site for residue PO4 A 503

Chain	Residue
A	ASP251
A	GLU254
B	GLN11
B	GLU69
B	THR143
B	GDP501

site_id	AC5
Number of Residues	5
Details	binding site for residue PO4 G 501

Chain	Residue
G	GLN11
G	GLU69
G	ALA97
G	THR143
G	GDP502

site_id	AC6
Number of Residues	13
Details	binding site for residue GDP G 502

Chain	Residue
G	GLY10
G	GLN11
G	CYS12
G	SER138
G	GLY141
G	GLY142
G	THR143
G	GLY144
G	ASP177
G	ASN204
G	TYR222
G	ASN226
G	PO4501

site_id	AC7
Number of Residues	14
Details	binding site for residue GDP D 501

Chain	Residue
C	LEU248
C	PO4501
D	GLY10
D	GLN11
D	CYS12
D	SER138
D	GLY141
D	GLY142
D	THR143
D	GLY144
D	ASP177
D	ASN204
D	TYR222
D	ASN226

site_id	AC8
Number of Residues	4
Details	binding site for residue PO4 I 501

Chain	Residue
I	GLN11
I	GLU69
I	THR143
I	GDP502

site_id	AC9
Number of Residues	13
Details	binding site for residue GDP I 502

Chain	Residue
I	GLY10
I	GLN11
I	CYS12
I	SER138
I	GLY141
I	GLY142
I	THR143
I	GLY144
I	ASP177
I	ASN204
I	TYR222
I	ASN226
I	PO4501

site_id	AD1
Number of Residues	14
Details	binding site for residue GDP B 501

Chain	Residue
B	ASP177
B	ASN204
B	TYR222
B	ASN226
A	LEU248
A	PO4503
B	GLY10
B	GLN11
B	CYS12
B	SER138
B	GLY141
B	GLY142
B	THR143
B	GLY144

site_id	AD2
Number of Residues	4
Details	binding site for residue PO4 H 501

Chain	Residue
H	GLN11
H	ALA97
H	THR143
H	GDP502

site_id	AD3
Number of Residues	13
Details	binding site for residue GDP H 502

Chain	Residue
H	GLY10
H	GLN11
H	CYS12
H	SER138
H	GLY141
H	GLY142
H	THR143
H	GLY144
H	ASP177
H	ASN204
H	TYR222
H	ASN226
H	PO4501

site_id	AD4
Number of Residues	6
Details	binding site for residue PO4 E 501

Chain	Residue
E	ASP251
E	GLU254
F	GLN11
F	GLU69
F	ALA97
F	GDP501

site_id	AD5
Number of Residues	18
Details	binding site for residue GTP E 502

Chain	Residue
E	GLY10
E	GLN11
E	ALA12
E	GLN15
E	GLU71
E	ALA99
E	ALA100
E	ASN101
E	SER140
E	GLY143
E	GLY144
E	THR145
E	GLY146
E	ASN206
E	TYR224
E	ASN228
E	ILE231
E	MG503

site_id	AD6
Number of Residues	3
Details	binding site for residue MG E 503

Chain	Residue
E	GLN11
E	GLU71
E	GTP502

site_id	AD7
Number of Residues	18
Details	binding site for residue GTP J 501

Chain	Residue
J	GLY10
J	GLN11
J	ALA12
J	GLN15
J	GLU71
J	ALA99
J	ALA100
J	ASN101
J	SER140
J	GLY143
J	GLY144
J	THR145
J	GLY146
J	ASN206
J	TYR224
J	ASN228
J	ILE231
J	MG502

site_id	AD8
Number of Residues	3
Details	binding site for residue MG J 502

Chain	Residue
J	GLN11
J	GLU71
J	GTP501

site_id	AD9
Number of Residues	6
Details	binding site for residue PO4 C 501

Chain	Residue
C	ASP251
C	GLU254
D	GLN11
D	GLU69
D	THR143
D	GDP501

site_id	AE1
Number of Residues	19
Details	binding site for residue GTP C 502

Chain	Residue
C	GLY10
C	GLN11
C	ALA12
C	GLN15
C	GLU71
C	ALA99
C	ALA100
C	ASN101
C	SER140
C	GLY143
C	GLY144
C	THR145
C	GLY146
C	ASN206
C	TYR224
C	ASN228
C	ILE231
C	MG503
I	LYS252

site_id	AE2
Number of Residues	3
Details	binding site for residue MG C 503

Chain	Residue
C	GLN11
C	GLU71
C	GTP502

site_id	AE3
Number of Residues	18
Details	binding site for residue GTP L 501

Chain	Residue
L	GLY10
L	GLN11
L	ALA12
L	GLN15
L	GLU71
L	ALA99
L	ALA100
L	ASN101
L	SER140
L	GLY143
L	GLY144
L	THR145
L	GLY146
L	ASN206
L	TYR224
L	ASN228
L	ILE231
L	MG502

site_id	AE4
Number of Residues	3
Details	binding site for residue MG L 502

Chain	Residue
L	GLN11
L	GLU71
L	GTP501

site_id	AE5
Number of Residues	18
Details	binding site for residue GTP K 501

Chain	Residue
K	GLY10
K	GLN11
K	ALA12
K	GLN15
K	GLU71
K	ALA99
K	ALA100
K	ASN101
K	SER140
K	GLY143
K	GLY144
K	THR145
K	GLY146
K	ASN206
K	TYR224
K	ASN228
K	ILE231
K	MG502

site_id	AE6
Number of Residues	3
Details	binding site for residue MG K 502

Chain	Residue
K	GLN11
K	GLU71
K	GTP501

Functional Information from PROSITE/UniProt

site_id	PS00227
Number of Residues	7
Details	TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG

Chain	Residue	Details
F	GLY140-GLY146
A	GLY142-GLY148

site_id	PS00228
Number of Residues	4
Details	TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI

Chain	Residue	Details
F	MET1-ILE4

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: ACT_SITE => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	GLU254
G	GLY142
G	THR143
G	GLY144
G	ASN204
G	ASN226
D	GLN11
D	SER138
D	GLY142
D	THR143
D	GLY144
E	GLU254
D	ASN204
D	ASN226
I	GLN11
I	SER138
I	GLY142
I	THR143
I	GLY144
I	ASN204
I	ASN226
B	GLN11
J	GLU254
B	SER138
B	GLY142
B	THR143
B	GLY144
B	ASN204
B	ASN226
H	GLN11
H	SER138
H	GLY142
H	THR143
C	GLU254
H	GLY144
H	ASN204
H	ASN226
L	GLU254
K	GLU254
F	ASN226
G	GLN11
G	SER138

site_id	SWS_FT_FI2
Number of Residues	48
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	GLN11
E	GLU71
E	SER140
E	GLY144
E	THR145
E	THR179
E	ASN206
E	ASN228
J	GLN11
J	GLU71
J	SER140
A	GLU71
J	GLY144
J	THR145
J	THR179
J	ASN206
J	ASN228
C	GLN11
C	GLU71
C	SER140
C	GLY144
C	THR145
A	SER140
C	THR179
C	ASN206
C	ASN228
L	GLN11
L	GLU71
L	SER140
L	GLY144
L	THR145
L	THR179
L	ASN206
A	GLY144
L	ASN228
K	GLN11
K	GLU71
K	SER140
K	GLY144
K	THR145
K	THR179
K	ASN206
K	ASN228
A	THR145
A	THR179
A	ASN206
A	ASN228
E	GLN11

site_id	SWS_FT_FI3
Number of Residues	6
Details	SITE: Involved in polymerization => ECO:0000250

Chain	Residue	Details
A	TYR451
E	TYR451
J	TYR451
C	TYR451
L	TYR451
K	TYR451

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	LYS40
E	LYS40
J	LYS40
C	LYS40
L	LYS40
K	LYS40

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	SER48
L	SER232
K	SER48
K	SER232
A	SER232
E	SER48
E	SER232
J	SER48
J	SER232
C	SER48
C	SER232
L	SER48

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: 3'-nitrotyrosine => ECO:0000250\|UniProtKB:P68373

Chain	Residue	Details
A	TYR282
B	THR290
H	THR285
H	THR290
E	TYR282
J	TYR282
C	TYR282
L	TYR282
K	TYR282
I	THR285
I	THR290
B	THR285

site_id	SWS_FT_FI7
Number of Residues	6
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	ARG339
E	ARG339
J	ARG339
C	ARG339
L	ARG339
K	ARG339

site_id	SWS_FT_FI8
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P68373

Chain	Residue	Details
A	SER439
E	SER439
J	SER439
C	SER439
L	SER439
K	SER439

site_id	SWS_FT_FI9
Number of Residues	6
Details	MOD_RES: 5-glutamyl polyglutamate => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	GLU443
E	GLU443
J	GLU443
C	GLU443
L	GLU443
K	GLU443

site_id	SWS_FT_FI10
Number of Residues	6
Details	MOD_RES: 5-glutamyl polyglutamate => ECO:0000250\|UniProtKB:P68369

Chain	Residue	Details
A	GLU445
B	LYS324
H	LYS324
E	GLU445
J	GLU445
C	GLU445
L	GLU445
K	GLU445
I	LYS324

site_id	SWS_FT_FI11
Number of Residues	6
Details	MOD_RES: 3'-nitrotyrosine => ECO:0000250\|UniProtKB:Q71U36

Chain	Residue	Details
A	TYR451
E	TYR451
J	TYR451
C	TYR451
L	TYR451
K	TYR451

site_id	SWS_FT_FI12
Number of Residues	18
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	LYS326
C	LYS326
C	LYS370
L	LYS326
L	LYS370
K	LYS326
K	LYS370
A	LYS370
E	LYS326
E	LYS370
J	LYS326
J	LYS370

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)