Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3JAT

Cryo-EM structure of GMPCPP-microtubule (14 protofilaments) decorated with kinesin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0000166	molecular_function	nucleotide 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	0000166	molecular_function	nucleotide 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	0000166	molecular_function	nucleotide 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	0000166	molecular_function	nucleotide 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	0000166	molecular_function	nucleotide 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	0000166	molecular_function	nucleotide 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	0000166	molecular_function	nucleotide 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	0000166	molecular_function	nucleotide 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	0000166	molecular_function	nucleotide 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	0000166	molecular_function	nucleotide 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	0000166	molecular_function	nucleotide 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	20
Details	BINDING SITE FOR RESIDUE GTP E 501

Chain	Residue
E	GLY10
E	GLY144
E	THR145
E	GLY146
E	ILE171
E	THR179
E	GLU183
E	ASN206
E	TYR224
E	ASN228
E	MG502
E	GLN11
G	LYS254
E	ALA12
E	GLN15
E	ALA99
E	ALA100
E	ASN101
E	SER140
E	GLY143

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG E 502

Chain	Residue
E	GLU71
E	GTP501

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE G2P F 501

Chain	Residue
E	GLU254
F	GLY10
F	GLN11
F	CYS12
F	GLN15
F	ALA99
F	ASN101
F	GLY144
F	THR145
F	GLY146
F	ASN206
F	TYR224
F	ASN228
F	MG502

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG F 502

Chain	Residue
F	G2P501

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE GTP J 501

Chain	Residue
F	LYS254
J	GLY10
J	GLN11
J	ALA12
J	GLN15
J	ASP98
J	ALA99
J	ALA100
J	ASN101
J	SER140
J	GLY144
J	THR145
J	GLY146
J	ILE171
J	THR179
J	GLU183
J	ASN206
J	TYR224
J	ASN228
J	MG502

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG J 502

Chain	Residue
J	GTP501

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE G2P G 501

Chain	Residue
G	GLY10
G	GLN11
G	CYS12
G	GLN15
G	ALA99
G	ASN101
G	GLY144
G	THR145
G	GLY146
G	GLU183
G	ASN206
G	TYR224
G	ASN228
G	MG502

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG G 502

Chain	Residue
G	G2P501

site_id	AC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE GTP C 501

Chain	Residue
C	GLY10
C	GLN11
C	ALA12
C	GLN15
C	ALA99
C	ALA100
C	ASN101
C	SER140
C	GLY143
C	GLY144
C	THR145
C	GLY146
C	THR179
C	GLU183
C	ASN206
C	TYR224
C	ASN228
C	MG502
I	LYS254

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG C 502

Chain	Residue
C	GLU71
C	GTP501

site_id	BC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE G2P D 501

Chain	Residue
D	ALA99
D	ASN101
D	GLY144
D	THR145
D	GLY146
D	ASP179
D	GLU183
D	ASN206
D	TYR224
D	ASN228
D	MG502
C	GLU254
D	GLY10
D	GLN11
D	CYS12
D	GLN15

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG D 502

Chain	Residue
D	G2P501

site_id	BC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE GTP L 501

Chain	Residue
D	LYS254
L	GLY10
L	GLN11
L	ALA12
L	GLN15
L	ALA99
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	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG L 502

Chain	Residue
L	GLU71
L	GTP501

site_id	BC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE G2P I 501

Chain	Residue
I	GLY10
I	GLN11
I	CYS12
I	GLN15
I	ALA99
I	ASN101
I	GLY144
I	THR145
I	GLY146
I	GLU183
I	ASN206
I	TYR224
I	ASN228
I	MG502

site_id	BC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG I 502

Chain	Residue
I	G2P501

site_id	BC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE GTP A 501

Chain	Residue
A	GLY10
A	GLN11
A	ALA12
A	GLN15
A	ALA99
A	ASN101
A	SER140
A	GLY143
A	GLY144
A	THR145
A	GLY146
A	ILE171
A	THR179
A	GLU183
A	ASN206
A	TYR224
A	ASN228
A	MG502
H	LYS254

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 502

Chain	Residue
A	GLU71
A	GTP501

site_id	CC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE G2P B 501

Chain	Residue
A	GLU254
B	GLY10
B	GLN11
B	CYS12
B	GLN15
B	ALA99
B	ASN101
B	GLY144
B	THR145
B	GLY146
B	ASP179
B	GLU183
B	ASN206
B	TYR224
B	ASN228
B	MG502

site_id	CC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG B 502

Chain	Residue
B	G2P501

site_id	CC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE GTP K 501

Chain	Residue
B	LYS254
K	GLY10
K	GLN11
K	ALA12
K	GLN15
K	ALA99
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	CC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG K 502

Chain	Residue
K	GTP501

site_id	CC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE G2P H 501

Chain	Residue
H	GLY10
H	GLN11
H	CYS12
H	GLN15
H	ALA99
H	ASN101
H	GLY144
H	THR145
H	GLY146
H	GLU183
H	ASN206
H	TYR224
H	ASN228
H	MG502

site_id	CC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG H 502

Chain	Residue
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
E	GLY142-GLY148
F	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	42
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q13509

Chain	Residue	Details
F	GLN11
G	GLY144
G	THR145
G	GLY146
G	ASN206
G	ASN228
D	GLN11
D	SER140
D	GLY144
D	THR145
D	GLY146
F	SER140
D	ASN206
D	ASN228
I	GLN11
I	SER140
I	GLY144
I	THR145
I	GLY146
I	ASN206
I	ASN228
B	GLN11
F	GLY144
B	SER140
B	GLY144
B	THR145
B	GLY146
B	ASN206
B	ASN228
H	GLN11
H	SER140
H	GLY144
H	THR145
F	THR145
H	GLY146
H	ASN206
H	ASN228
F	GLY146
F	ASN206
F	ASN228
G	GLN11
G	SER140

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

Chain	Residue	Details
F	GLU71
J	GLU71
J	SER140
J	GLY144
J	THR145
J	THR179
J	ASN206
J	ASN228
C	GLN11
C	GLU71
C	SER140
G	GLU71
C	GLY144
C	THR145
C	THR179
C	ASN206
C	ASN228
L	GLN11
L	GLU71
L	SER140
L	GLY144
L	THR145
D	GLU71
L	THR179
L	ASN206
L	ASN228
A	GLN11
A	GLU71
A	SER140
A	GLY144
A	THR145
A	THR179
A	ASN206
I	GLU71
A	ASN228
K	GLN11
K	GLU71
K	SER140
K	GLY144
K	THR145
K	THR179
K	ASN206
K	ASN228
B	GLU71
H	GLU71
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
F	SER40
G	SER40
D	SER40
I	SER40
B	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
F	LYS60
G	LYS60
D	LYS60
I	LYS60
B	LYS60
H	LYS60

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

Chain	Residue	Details
F	SER174
A	SER232
K	SER48
K	SER232
G	SER174
D	SER174
I	SER174
B	SER174
H	SER174
L	SER48
L	SER232
A	SER48

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

Chain	Residue	Details
F	THR287
B	THR292
H	THR287
H	THR292
F	THR292
G	THR287
G	THR292
D	THR287
D	THR292
I	THR287
I	THR292
B	THR287

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

Chain	Residue	Details
F	ARG320
G	ARG320
D	ARG320
I	ARG320
B	ARG320
H	ARG320

site_id	SWS_FT_FI8
Number of Residues	6
Details	MOD_RES: 5-glutamyl polyglutamate => ECO:0000250\|UniProtKB:Q2T9S0

Chain	Residue	Details
F	GLU448
G	GLU448
D	GLU448
I	GLU448
B	GLU448
H	GLU448

site_id	SWS_FT_FI9
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
F	LYS60
G	LYS60
D	LYS60
I	LYS60
B	LYS60
H	LYS60

site_id	SWS_FT_FI10
Number of Residues	12
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:P07437

Chain	Residue	Details
E	GLU445
B	LYS326
H	LYS326
F	LYS326
C	GLU445
G	LYS326
A	GLU445
D	LYS326
I	LYS326

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

Chain	Residue	Details
E	TYR451
J	TYR451
C	TYR451
L	TYR451
A	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
E	LYS326
L	LYS326
L	LYS370
A	LYS326
A	LYS370
K	LYS326
K	LYS370
E	LYS370
J	LYS326
J	LYS370
C	LYS326
C	LYS370

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