Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3E22

Tubulin-colchicine-soblidotin: Stathmin-like domain complex

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	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	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	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	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	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	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GTP A 600

Chain	Residue
A	GLN11
A	GLY143
A	GLY144
A	THR145
A	GLY146
A	ILE171
A	PRO173
A	SER178
A	GLU183
A	ASN206
A	TYR224
A	ALA12
A	ASN228
B	LYS254
A	GLN15
A	ILE16
A	ASP69
A	GLU71
A	ASP98
A	SER140
A	GLY142

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 601

Chain	Residue
A	ASP98
A	ASN101
A	GLY144
A	THR145

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GDP B 600

Chain	Residue
B	GLY10
B	GLN11
B	CYS12
B	ASN101
B	SER140
B	GLY144
B	THR145
B	GLY146
B	PRO173
B	SER178
B	GLU183
B	ASN206
B	TYR224
B	ASN228

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE LOC B 700

Chain	Residue
A	SER178
A	THR179
A	ALA180
B	THR239
B	CYS241
B	LEU242
B	LEU248
B	ALA250
B	LYS254
B	LEU255
B	ASN258
B	ALA316
B	ASN350
B	LYS352

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TZT B 800

Chain	Residue
B	GLN11
B	GLN15
B	THR74
B	SER178
B	ASP179
B	PRO222
B	THR223
B	TYR224
B	GLY225
C	PRO325
C	ASN329
C	PHE351

site_id	AC6
Number of Residues	22
Details	BINDING SITE FOR RESIDUE GTP C 600

Chain	Residue
C	GLY10
C	GLN11
C	ALA12
C	GLN15
C	ILE16
C	ASP69
C	GLU71
C	ASP98
C	SER140
C	GLY142
C	GLY143
C	GLY144
C	THR145
C	GLY146
C	ILE171
C	PRO173
C	SER178
C	GLU183
C	ASN206
C	TYR224
C	ASN228
D	LYS254

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 601

Chain	Residue
C	ASP98
C	ASN101
C	GLY144
C	THR145

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GDP D 600

Chain	Residue
D	GLY146
D	SER178
D	ASP179
D	GLU183
D	ASN206
D	TYR224
D	ASN228
D	GLY10
D	GLN11
D	CYS12
D	ASN101
D	SER140
D	GLY142
D	GLY144
D	THR145

site_id	AC9
Number of Residues	13
Details	BINDING SITE FOR RESIDUE LOC D 700

Chain	Residue
C	THR179
C	ALA180
D	THR239
D	CYS241
D	LEU242
D	LEU248
D	ALA250
D	LYS254
D	LEU255
D	ASN258
D	ALA316
D	ASN350
D	LYS352

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	1
Details	Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9BQE3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q3KRE8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
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_FI9
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_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
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_FI12
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_FI13
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_FI14
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)