Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4YJ2

Crystal structure of tubulin bound to MI-181

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	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	0005929	cellular_component	cilium
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	0000166	molecular_function	nucleotide binding
B	0000226	biological_process	microtubule cytoskeleton organization
B	0000278	biological_process	mitotic cell cycle
B	0001764	biological_process	neuron migration
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	0000166	molecular_function	nucleotide binding
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	0005929	cellular_component	cilium
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	0000166	molecular_function	nucleotide binding
D	0000226	biological_process	microtubule cytoskeleton organization
D	0000278	biological_process	mitotic cell cycle
D	0001764	biological_process	neuron migration
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
E	0031110	biological_process	regulation of microtubule polymerization or depolymerization
F	0036211	biological_process	protein modification process

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	binding site for residue GTP A 501

Chain	Residue
A	GLY10
A	GLY143
A	GLY144
A	THR145
A	GLY146
A	VAL177
A	SER178
A	GLU183
A	ASN206
A	TYR224
A	ASN228
A	GLN11
A	ILE231
A	MG502
A	HOH604
A	HOH610
A	HOH611
A	HOH615
A	HOH618
B	LYS254
A	ALA12
A	GLN15
A	ASP98
A	ALA99
A	ALA100
A	ASN101
A	SER140

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 502

Chain	Residue
A	GLU71
A	GTP501
A	HOH604
A	HOH611
A	HOH615
A	HOH618

site_id	AC3
Number of Residues	5
Details	binding site for residue CA A 503

Chain	Residue
A	ASP39
A	THR41
A	GLY44
A	GLU55
A	HOH601

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 504

Chain	Residue
A	ASN216
A	PRO274
A	VAL275
A	ALA294
A	ASN300

site_id	AC5
Number of Residues	5
Details	binding site for residue GOL A 505

Chain	Residue
A	HIS309
A	THR382
A	ALA383
A	GLU386
F	ARG66

site_id	AC6
Number of Residues	22
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	VAL177
B	ASP179
B	GLU183
B	ASN206
B	TYR224
B	ASN228
B	MG502
B	HOH603
B	HOH604
B	HOH606
B	HOH609
B	HOH620
B	HOH621

site_id	AC7
Number of Residues	6
Details	binding site for residue MG B 502

Chain	Residue
B	GLN11
B	GDP501
B	HOH605
B	HOH621
B	HOH626
C	HOH632

site_id	AC8
Number of Residues	4
Details	binding site for residue CA B 503

Chain	Residue
B	GLU113
B	HOH613
C	HOH635
C	HOH647

site_id	AC9
Number of Residues	13
Details	binding site for residue 4ED B 504

Chain	Residue
B	GLN136
B	ASN167
B	GLU200
B	TYR202
B	VAL238
B	THR239
B	CYS241
B	LEU242
B	LEU252
B	LEU255
B	ALA316
B	ILE318
B	HOH602

site_id	AD1
Number of Residues	7
Details	binding site for residue MES B 505

Chain	Residue
B	ARG253
B	ARG158
B	ASP163
B	ARG164
B	ILE165
B	ASN197
B	ASP199

site_id	AD2
Number of Residues	9
Details	binding site for residue MES B 506

Chain	Residue
B	PHE296
B	ASP297
B	SER298
B	ARG308
B	TYR312
B	VAL335
B	ASN339
B	TYR342
B	HOH601

site_id	AD3
Number of Residues	3
Details	binding site for residue GOL B 507

Chain	Residue
B	PRO222
B	TYR224
B	HOH629

site_id	AD4
Number of Residues	29
Details	binding site for residue GTP C 501

Chain	Residue
C	GLY10
C	GLN11
C	ALA12
C	GLN15
C	ASP69
C	ASP98
C	ALA99
C	ALA100
C	ASN101
C	SER140
C	GLY143
C	GLY144
C	THR145
C	GLY146
C	ILE171
C	VAL177
C	GLU183
C	ASN206
C	TYR224
C	ASN228
C	ILE231
C	MG505
C	HOH611
C	HOH612
C	HOH620
C	HOH622
C	HOH629
C	HOH637
D	LYS254

site_id	AD5
Number of Residues	5
Details	binding site for residue CA C 502

Chain	Residue
C	ASP39
C	THR41
C	GLY44
C	GLU55
C	HOH609

site_id	AD6
Number of Residues	4
Details	binding site for residue GOL C 503

Chain	Residue
C	ARG221
C	THR223
C	TYR224
D	GLN247

site_id	AD7
Number of Residues	2
Details	binding site for residue IMD C 504

Chain	Residue
C	ASP431
C	HOH643

site_id	AD8
Number of Residues	5
Details	binding site for residue MG C 505

Chain	Residue
C	GTP501
C	HOH611
C	HOH620
C	HOH629
C	HOH637

site_id	AD9
Number of Residues	17
Details	binding site for residue GDP D 501

Chain	Residue
D	GLY10
D	GLN11
D	CYS12
D	GLN15
D	ASN101
D	SER140
D	GLY143
D	GLY144
D	THR145
D	GLY146
D	VAL177
D	GLU183
D	ASN206
D	TYR224
D	ASN228
D	MG502
D	HOH605

site_id	AE1
Number of Residues	5
Details	binding site for residue MG D 502

Chain	Residue
D	GLN11
D	ASP179
D	GDP501
D	HOH602
D	HOH608

site_id	AE2
Number of Residues	18
Details	binding site for residue 4ED D 503

Chain	Residue
D	GLN136
D	ASN167
D	PHE169
D	GLU200
D	TYR202
D	VAL238
D	THR239
D	CYS241
D	LEU242
D	LEU248
D	ASN249
D	LEU252
D	LEU255
D	ALA316
D	ILE318
D	ALA354
D	ILE378
D	HOH607

site_id	AE3
Number of Residues	7
Details	binding site for residue GOL D 504

Chain	Residue
C	TRP407
D	ARG158
D	ASP163
D	ARG164
D	ILE165
D	ASP199
D	ARG253

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	GLY142-GLY148
A	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

site_id	PS00563
Number of Residues	10
Details	STATHMIN_1 Stathmin family signature 1. PRRRDpSLEE

Chain	Residue	Details
E	PRO40-GLU49

site_id	PS01041
Number of Residues	10
Details	STATHMIN_2 Stathmin family signature 2. AEKREHEREV

Chain	Residue	Details
E	ALA73-VAL82

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	6
Details	Motif: {"description":"MREI motif","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q3KRE8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"UniProtKB","id":"Q9BVA1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)