Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ZOL

Crystal Structure of Tubulin-Stathmin-TTL-Tubulysin M 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	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	0001764	biological_process	neuron migration
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	0001764	biological_process	neuron migration
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	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	GLY144
A	THR145
A	GLY146
A	VAL177
A	GLU183
A	ASN206
A	TYR224
A	ASN228
A	ILE231
A	MG502
A	GLN11
A	HOH615
A	HOH623
A	HOH632
A	HOH634
A	HOH646
A	HOH653
A	HOH655
B	LYS254
A	ALA12
A	GLN15
A	ASP98
A	ALA99
A	ASN101
A	SER140
A	GLY143

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 502

Chain	Residue
A	GTP501
A	HOH623
A	HOH632
A	HOH634
A	HOH646
B	LYS254

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	HOH603

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 504

Chain	Residue
A	SER158
A	GLY162
A	LYS166
A	GLU196
A	ASP199
A	HOH619
E	ASP44

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 505

Chain	Residue
A	ASN216
A	PRO274
A	VAL275
A	ILE276
A	ASN300
A	HOH641

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 506

Chain	Residue
A	ALA208
A	ASP211
A	ILE212
A	ARG215
A	PRO298
A	ALA299
A	GLN301
A	LYS304
F	GOL402

site_id	AC7
Number of Residues	23
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	SER178
B	GLU183
B	ASN206
B	TYR224
B	ASN228
B	MG502
B	55Q507
B	HOH601
B	HOH606
B	HOH607
B	HOH613
B	HOH620
B	HOH628

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 502

Chain	Residue
B	GLU71
B	GDP501
B	HOH620
B	HOH629
B	HOH655
B	HOH663

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MES B 503

Chain	Residue
B	PHE296
B	ASP297
B	ALA298
B	ARG308
B	ASN339
B	TYR342

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MES B 504

Chain	Residue
B	ASN197
B	THR198
B	ASP199
B	ARG253
B	HOH615
B	ARG158
B	ASP163
B	ARG164
B	ILE165

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 505

Chain	Residue
B	ASP116
B	ASP120
C	ASP218
C	GLU220

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 506

Chain	Residue
B	ARG401
C	GLU434
C	GOL504

site_id	BC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 55Q B 507

Chain	Residue
B	GLN15
B	LYS176
B	ASP179
B	PRO222
B	THR223
B	TYR224
B	GLY225
B	ARG278
B	GDP501
B	HOH609
B	HOH618
C	ASN329
C	VAL353

site_id	BC5
Number of Residues	26
Details	BINDING SITE FOR RESIDUE GTP C 501

Chain	Residue
C	GLY10
C	GLN11
C	ALA12
C	GLN15
C	ASP98
C	ALA99
C	ASN101
C	SER140
C	GLY143
C	GLY144
C	THR145
C	GLY146
C	VAL177
C	GLU183
C	ASN206
C	TYR224
C	ASN228
C	ILE231
C	MG502
C	HOH606
C	HOH609
C	HOH627
C	HOH633
C	HOH662
C	HOH668
D	LYS254

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 502

Chain	Residue
C	GTP501
C	HOH606
C	HOH609
C	HOH633
C	HOH662

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 503

Chain	Residue
C	ASP39
C	THR41
C	GLY44
C	GLU55
C	HOH602

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 504

Chain	Residue
B	GOL506
C	ASP431
C	HOH678

site_id	BC9
Number of Residues	23
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	VAL177
D	SER178
D	GLU183
D	ASN206
D	TYR224
D	LEU227
D	ASN228
D	MG502
D	HOH601
D	HOH607
D	HOH609
D	HOH620
D	HOH624
D	HOH629

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 502

Chain	Residue
D	GDP501
D	HOH601
D	HOH604
D	HOH607
D	HOH609
D	HOH629

site_id	CC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 55Q D 503

Chain	Residue
D	GLN15
D	PRO175
D	LYS176
D	VAL177
D	ASP179
D	PRO222
D	THR223
D	TYR224
D	GLY225
D	ARG278

site_id	CC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ACP F 401

Chain	Residue
F	LYS74
F	ILE148
F	LYS150
F	GLN183
F	LYS184
F	TYR185
F	LEU186
F	LYS198
F	ASP200
F	ARG222
F	LEU240
F	THR241
F	ASN242
F	ASP318
F	GLU331
F	ASN333
F	HOH501

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL F 402

Chain	Residue
A	ARG215
A	GOL506
F	HIS306
F	LEU307
F	HIS308

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	6
Details	Motif: {"description":"MREC motif","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
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_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
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_FI7
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_FI8
Number of Residues	2
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	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_FI10
Number of Residues	6
Details	Motif: {"description":"MREI motif","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","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":"Q13885","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)