Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6WVM

High curvature lateral interaction within a 13-protofilament, Taxol stabilized microtubule

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000226	biological_process	microtubule cytoskeleton organization
A	0000278	biological_process	mitotic cell cycle
A	0003725	molecular_function	double-stranded RNA binding
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	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005874	cellular_component	microtubule
A	0005881	cellular_component	cytoplasmic microtubule
A	0007017	biological_process	microtubule-based process
A	0015630	cellular_component	microtubule cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0046872	molecular_function	metal ion binding
A	0071353	biological_process	cellular response to interleukin-4
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	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	0007399	biological_process	nervous system development
B	0015630	cellular_component	microtubule cytoskeleton
B	0046872	molecular_function	metal ion binding
B	0046982	molecular_function	protein heterodimerization activity
B	1902669	biological_process	positive regulation of axon guidance
C	0000226	biological_process	microtubule cytoskeleton organization
C	0000278	biological_process	mitotic cell cycle
C	0003725	molecular_function	double-stranded RNA binding
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	0005829	cellular_component	cytosol
C	0005856	cellular_component	cytoskeleton
C	0005874	cellular_component	microtubule
C	0005881	cellular_component	cytoplasmic microtubule
C	0007017	biological_process	microtubule-based process
C	0015630	cellular_component	microtubule cytoskeleton
C	0016787	molecular_function	hydrolase activity
C	0031625	molecular_function	ubiquitin protein ligase binding
C	0046872	molecular_function	metal ion binding
C	0071353	biological_process	cellular response to interleukin-4
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	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	0007399	biological_process	nervous system development
D	0015630	cellular_component	microtubule cytoskeleton
D	0046872	molecular_function	metal ion binding
D	0046982	molecular_function	protein heterodimerization activity
D	1902669	biological_process	positive regulation of axon guidance

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	binding site for residue GTP C 501

Chain	Residue
C	GLY10
C	GLY143
C	GLY144
C	THR145
C	GLY146
C	ILE171
C	THR179
C	GLU183
C	ASN206
C	TYR224
C	LEU227
C	GLN11
C	ASN228
C	MG502
D	LYS254
C	ALA12
C	GLN15
C	ASP98
C	ALA99
C	ALA100
C	ASN101
C	SER140

site_id	AC2
Number of Residues	1
Details	binding site for residue MG C 502

Chain	Residue
C	GTP501

site_id	AC3
Number of Residues	14
Details	binding site for residue GDP D 501

Chain	Residue
D	GLY10
D	GLN11
D	CYS12
D	GLN15
D	SER140
D	GLY143
D	GLY144
D	THR145
D	GLY146
D	ASP179
D	GLU183
D	ASN206
D	TYR224
D	ASN228

site_id	AC4
Number of Residues	17
Details	binding site for residue TA1 D 502

Chain	Residue
D	GLU22
D	VAL23
D	ASP26
D	GLU27
D	ASP226
D	HIS229
D	ALA233
D	SER236
D	PHE272
D	PRO274
D	LEU275
D	THR276
D	ARG278
D	GLN281
D	ARG369
D	GLY370
D	LEU371

site_id	AC5
Number of Residues	22
Details	binding site for residue GTP A 501

Chain	Residue
A	GLY10
A	GLN11
A	ALA12
A	GLN15
A	ASP98
A	ALA99
A	ALA100
A	ASN101
A	SER140
A	GLY143
A	GLY144
A	THR145
A	GLY146
A	ILE171
A	THR179
A	GLU183
A	ASN206
A	TYR224
A	LEU227
A	ASN228
A	MG502
B	LYS254

site_id	AC6
Number of Residues	1
Details	binding site for residue MG A 502

Chain	Residue
A	GTP501

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

Chain	Residue
B	GLY10
B	GLN11
B	CYS12
B	GLN15
B	SER140
B	GLY143
B	GLY144
B	THR145
B	GLY146
B	ASP179
B	GLU183
B	ASN206
B	TYR224
B	ASN228

site_id	AC8
Number of Residues	17
Details	binding site for residue TA1 B 502

Chain	Residue
B	PHE272
B	PRO274
B	LEU275
B	THR276
B	GLN281
B	PRO360
B	ARG369
B	GLY370
B	LEU371
B	GLU22
B	VAL23
B	ASP26
B	LEU217
B	ASP226
B	HIS229
B	ALA233
B	SER236

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
D	GLY142-GLY148
C	GLY142-GLY148

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

Chain	Residue	Details
D	MET1-ILE4

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q13509

Chain	Residue	Details
D	GLN11
B	GLY144
B	THR145
B	GLY146
B	ASN206
B	ASN228
D	SER140
D	GLY144
D	THR145
D	GLY146
D	ASN206
D	ASN228
B	GLN11
B	SER140

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
D	GLU71
A	GLU71
A	SER140
A	GLY144
A	THR145
A	THR179
A	ASN206
A	ASN228
B	GLU71
C	SER140
C	GLY144
C	THR145
C	THR179
C	ASN206
C	ASN228
A	GLN11

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P99024

Chain	Residue	Details
D	SER40
B	SER40

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:Q3KRE8

Chain	Residue	Details
D	ALA57
B	ALA57

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P99024

Chain	Residue	Details
D	LYS60
B	LYS60
A	SER48
A	SER232

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine; by CDK1 => ECO:0000250\|UniProtKB:Q9BVA1

Chain	Residue	Details
D	SER174
B	SER174

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P07437

Chain	Residue	Details
D	THR287
D	THR292
B	THR287
B	THR292

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250\|UniProtKB:P07437

Chain	Residue	Details
D	ARG320
B	ARG320

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: 5-glutamyl polyglutamate => ECO:0000250\|UniProtKB:Q2T9S0

Chain	Residue	Details
D	GLU448
B	GLU448

site_id	SWS_FT_FI10
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250\|UniProtKB:P07437

Chain	Residue	Details
D	LYS60
B	LYS60

site_id	SWS_FT_FI11
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:P07437

Chain	Residue	Details
C	TYR451
D	LYS326
B	LYS326

site_id	SWS_FT_FI12
Number of Residues	6
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
C	LYS326
C	LYS370
A	LYS326
A	LYS370

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