Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6EVW

Cryo-EM structure of GMPCPP-microtubule 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	19
Details	binding site for residue GTP E 501

Chain	Residue
E	GLY10
E	GLY142
E	GLY143
E	GLY144
E	THR145
E	GLY146
E	ILE171
E	GLU183
E	TYR224
E	ASN228
E	MG502
E	GLN11
E	ALA12
E	GLN15
E	ASP98
E	ALA99
E	ALA100
E	ASN101
E	SER140

site_id	AC2
Number of Residues	3
Details	binding site for residue MG E 502

Chain	Residue
E	GLN11
E	GLU71
E	GTP501

site_id	AC3
Number of Residues	21
Details	binding site for residue GTP J 501

Chain	Residue
J	GLY10
J	GLN11
J	ALA12
J	GLN15
J	ILE16
J	ASP98
J	ALA99
J	ALA100
J	ASN101
J	SER140
J	GLY143
J	GLY144
J	THR145
J	GLY146
J	ILE171
J	THR179
J	GLU183
J	ASN206
J	TYR224
J	ASN228
J	MG502

site_id	AC4
Number of Residues	3
Details	binding site for residue MG J 502

Chain	Residue
J	GLN11
J	GLU71
J	GTP501

site_id	AC5
Number of Residues	18
Details	binding site for residue GTP C 501

Chain	Residue
C	GLN11
C	ALA12
C	GLN15
C	ILE16
C	ASP98
C	ALA100
C	ASN101
C	SER140
C	GLY142
C	GLY143
C	GLY144
C	THR145
C	GLY146
C	ILE171
C	GLU183
C	TYR224
C	ASN228
C	MG502

site_id	AC6
Number of Residues	3
Details	binding site for residue MG C 502

Chain	Residue
C	GLN11
C	GLU71
C	GTP501

site_id	AC7
Number of Residues	19
Details	binding site for residue GTP L 501

Chain	Residue
L	GLN11
L	ALA12
L	GLN15
L	ILE16
L	ASP98
L	ALA100
L	ASN101
L	SER140
L	GLY143
L	GLY144
L	THR145
L	GLY146
L	ILE171
L	THR179
L	GLU183
L	ASN206
L	TYR224
L	ASN228
L	MG502

site_id	AC8
Number of Residues	3
Details	binding site for residue MG L 502

Chain	Residue
L	GLN11
L	GLU71
L	GTP501

site_id	AC9
Number of Residues	18
Details	binding site for residue GTP A 501

Chain	Residue
A	GLY144
A	THR145
A	GLY146
A	ILE171
A	GLU183
A	TYR224
A	ASN228
A	MG502
A	GLN11
A	ALA12
A	GLN15
A	ILE16
A	ASP98
A	ALA100
A	ASN101
A	SER140
A	GLY142
A	GLY143

site_id	AD1
Number of Residues	3
Details	binding site for residue MG A 502

Chain	Residue
A	GLN11
A	GLU71
A	GTP501

site_id	AD2
Number of Residues	19
Details	binding site for residue GTP K 501

Chain	Residue
K	GLN11
K	ALA12
K	GLN15
K	ILE16
K	ASP98
K	ALA100
K	ASN101
K	SER140
K	GLY143
K	GLY144
K	THR145
K	GLY146
K	ILE171
K	THR179
K	GLU183
K	ASN206
K	TYR224
K	ASN228
K	MG502

site_id	AD3
Number of Residues	3
Details	binding site for residue MG K 502

Chain	Residue
K	GLN11
K	GLU71
K	GTP501

site_id	AD4
Number of Residues	18
Details	binding site for residue G2P B 501

Chain	Residue
A	GLU254
B	GLY10
B	GLN11
B	CYS12
B	GLN15
B	ALA97
B	GLY98
B	ASN99
B	SER138
B	GLY141
B	GLY142
B	THR143
B	GLY144
B	ASP177
B	THR178
B	TYR222
B	ASN226
B	MG502

site_id	AD5
Number of Residues	2
Details	binding site for residue MG B 502

Chain	Residue
B	GLN11
B	G2P501

site_id	AD6
Number of Residues	18
Details	binding site for residue G2P F 501

Chain	Residue
E	GLU254
F	GLY10
F	GLN11
F	CYS12
F	GLN15
F	ALA97
F	GLY98
F	ASN99
F	SER138
F	GLY141
F	GLY142
F	THR143
F	GLY144
F	ASP177
F	THR178
F	TYR222
F	ASN226
F	MG502

site_id	AD7
Number of Residues	2
Details	binding site for residue MG F 502

Chain	Residue
F	GLN11
F	G2P501

site_id	AD8
Number of Residues	17
Details	binding site for residue G2P G 501

Chain	Residue
G	GLY10
G	GLN11
G	CYS12
G	GLN15
G	ALA97
G	GLY98
G	ASN99
G	SER138
G	GLY141
G	GLY142
G	THR143
G	GLY144
G	ASP177
G	THR178
G	TYR222
G	ASN226
G	MG502

site_id	AD9
Number of Residues	2
Details	binding site for residue MG G 502

Chain	Residue
G	GLN11
G	G2P501

site_id	AE1
Number of Residues	18
Details	binding site for residue G2P D 501

Chain	Residue
C	GLU254
D	GLY10
D	GLN11
D	CYS12
D	GLN15
D	ALA97
D	GLY98
D	ASN99
D	SER138
D	GLY141
D	GLY142
D	THR143
D	GLY144
D	ASP177
D	THR178
D	TYR222
D	ASN226
D	MG502

site_id	AE2
Number of Residues	2
Details	binding site for residue MG D 502

Chain	Residue
D	GLN11
D	G2P501

site_id	AE3
Number of Residues	17
Details	binding site for residue G2P I 501

Chain	Residue
I	GLY10
I	GLN11
I	CYS12
I	GLN15
I	ALA97
I	GLY98
I	ASN99
I	SER138
I	GLY141
I	GLY142
I	THR143
I	GLY144
I	ASP177
I	THR178
I	TYR222
I	ASN226
I	MG502

site_id	AE4
Number of Residues	2
Details	binding site for residue MG I 502

Chain	Residue
I	GLN11
I	G2P501

site_id	AE5
Number of Residues	17
Details	binding site for residue G2P H 501

Chain	Residue
H	GLY10
H	GLN11
H	CYS12
H	GLN15
H	ALA97
H	GLY98
H	ASN99
H	SER138
H	GLY141
H	GLY142
H	THR143
H	GLY144
H	ASP177
H	THR178
H	TYR222
H	ASN226
H	MG502

site_id	AE6
Number of Residues	2
Details	binding site for residue MG H 502

Chain	Residue
H	GLN11
H	G2P501

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
B	GLY140-GLY146
E	GLY142-GLY148

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

Chain	Residue	Details
B	MET1-ILE4

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	42
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q13509

Chain	Residue	Details
B	GLN11
F	GLY142
F	THR143
F	GLY144
F	ASN204
F	ASN226
G	GLN11
G	SER138
G	GLY142
G	THR143
G	GLY144
B	SER138
G	ASN204
G	ASN226
D	GLN11
D	SER138
D	GLY142
D	THR143
D	GLY144
D	ASN204
D	ASN226
I	GLN11
B	GLY142
I	SER138
I	GLY142
I	THR143
I	GLY144
I	ASN204
I	ASN226
H	GLN11
H	SER138
H	GLY142
H	THR143
B	THR143
H	GLY144
H	ASN204
H	ASN226
B	GLY144
B	ASN204
B	ASN226
F	GLN11
F	SER138

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
B	GLU69
J	GLU71
J	SER140
J	GLY144
J	THR145
J	THR179
J	ASN206
J	ASN228
C	GLN11
C	GLU71
C	SER140
F	GLU69
C	GLY144
C	THR145
C	THR179
C	ASN206
C	ASN228
L	GLN11
L	GLU71
L	SER140
L	GLY144
L	THR145
G	GLU69
L	THR179
L	ASN206
L	ASN228
A	GLN11
A	GLU71
A	SER140
A	GLY144
A	THR145
A	THR179
A	ASN206
D	GLU69
A	ASN228
K	GLN11
K	GLU71
K	SER140
K	GLY144
K	THR145
K	THR179
K	ASN206
K	ASN228
I	GLU69
H	GLU69
E	ASN206
E	ASN228
J	GLN11

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P99024

Chain	Residue	Details
B	SER40
F	SER40
G	SER40
D	SER40
I	SER40
H	SER40

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P99024

Chain	Residue	Details
B	LYS58
A	SER232
K	SER48
K	SER232
F	LYS58
G	LYS58
D	LYS58
I	LYS58
H	LYS58
L	SER48
L	SER232
A	SER48

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: Phosphoserine; by CDK1 => ECO:0000250\|UniProtKB:Q13885

Chain	Residue	Details
B	SER172
F	SER172
G	SER172
D	SER172
I	SER172
H	SER172

site_id	SWS_FT_FI6
Number of Residues	12
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P07437

Chain	Residue	Details
B	THR285
I	THR290
H	THR285
H	THR290
B	THR290
F	THR285
F	THR290
G	THR285
G	THR290
D	THR285
D	THR290
I	THR285

site_id	SWS_FT_FI7
Number of Residues	6
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250\|UniProtKB:P07437

Chain	Residue	Details
B	ARG318
L	LYS326
L	LYS370
A	LYS326
A	LYS370
K	LYS326
K	LYS370
F	ARG318
G	ARG318
D	ARG318
I	ARG318
H	ARG318
C	LYS326
C	LYS370

site_id	SWS_FT_FI8
Number of Residues	6
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250\|UniProtKB:P07437

Chain	Residue	Details
B	LYS58
F	LYS58
G	LYS58
D	LYS58
I	LYS58
H	LYS58

site_id	SWS_FT_FI9
Number of Residues	12
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:P07437

Chain	Residue	Details
I	LYS324
H	LYS324
B	LYS324
F	LYS324
G	LYS324
D	LYS324

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