Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6TIZ

DROSOPHILA GDP-TUBULIN Y222F MUTANT

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000226	biological_process	microtubule cytoskeleton organization
A	0000235	cellular_component	astral microtubule
A	0000278	biological_process	mitotic cell cycle
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005525	molecular_function	GTP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005813	cellular_component	centrosome
A	0005819	cellular_component	spindle
A	0005856	cellular_component	cytoskeleton
A	0005874	cellular_component	microtubule
A	0007017	biological_process	microtubule-based process
A	0016787	molecular_function	hydrolase activity
A	0032418	biological_process	lysosome localization
A	0046872	molecular_function	metal ion binding
A	0048471	cellular_component	perinuclear region of cytoplasm
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	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	0000235	cellular_component	astral microtubule
C	0000278	biological_process	mitotic cell cycle
C	0005200	molecular_function	structural constituent of cytoskeleton
C	0005525	molecular_function	GTP binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005813	cellular_component	centrosome
C	0005819	cellular_component	spindle
C	0005856	cellular_component	cytoskeleton
C	0005874	cellular_component	microtubule
C	0007017	biological_process	microtubule-based process
C	0016787	molecular_function	hydrolase activity
C	0032418	biological_process	lysosome localization
C	0046872	molecular_function	metal ion binding
C	0048471	cellular_component	perinuclear region of cytoplasm
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	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	30
Details	binding site for residue GTP A 501

Chain	Residue
A	GLY10
A	GLY143
A	GLY144
A	THR145
A	GLY146
A	VAL177
A	THR179
A	GLU183
A	ASN206
A	TYR224
A	ASN228
A	GLN11
A	ILE231
A	MG502
A	HOH604
A	HOH633
A	HOH659
A	HOH669
A	HOH693
A	HOH705
A	HOH734
A	HOH738
A	ALA12
B	LYS252
A	GLN15
A	ASP98
A	ALA99
A	ALA100
A	ASN101
A	SER140

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 502

Chain	Residue
A	GTP501
A	HOH604
A	HOH659
A	HOH669
A	HOH738

site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 A 503

Chain	Residue
A	PRO175
A	LYS394
A	HOH723
B	ASN347

site_id	AC4
Number of Residues	7
Details	binding site for residue SO4 A 504

Chain	Residue
A	ARG308
A	ARG339
A	THR340
A	ILE341
A	HOH605
A	HOH678
A	HOH748

site_id	AC5
Number of Residues	5
Details	binding site for residue SO4 A 505

Chain	Residue
A	ASN216
A	LEU286
A	HOH625
A	HOH714
D	LYS122

site_id	AC6
Number of Residues	6
Details	binding site for residue GOL A 506

Chain	Residue
A	ARG105
A	GLY410
A	GLU411
A	HOH697
E	ARG61
E	GLU65

site_id	AC7
Number of Residues	4
Details	binding site for residue GOL A 507

Chain	Residue
A	VAL177
A	ARG221
A	THR223
A	TYR224

site_id	AC8
Number of Residues	24
Details	binding site for residue GDP B 501

Chain	Residue
B	GLY10
B	GLN11
B	CYS12
B	GLN15
B	SER138
B	GLY141
B	GLY142
B	THR143
B	GLY144
B	PRO171
B	VAL175
B	ASP177
B	GLU181
B	ASN204
B	PHE222
B	ASN226
B	HOH618
B	HOH619
B	HOH621
B	HOH628
B	HOH629
B	HOH646
B	HOH655
B	HOH684

site_id	AC9
Number of Residues	3
Details	binding site for residue SO4 B 502

Chain	Residue
B	THR221
B	GLY223
B	ARG276

site_id	AD1
Number of Residues	4
Details	binding site for residue SO4 B 503

Chain	Residue
B	LEU217
B	THR218
B	THR219
C	LYS326

site_id	AD2
Number of Residues	29
Details	binding site for residue GTP C 501

Chain	Residue
C	ASN101
C	SER140
C	GLY143
C	GLY144
C	THR145
C	GLY146
C	VAL177
C	THR179
C	GLU183
C	ASN206
C	TYR224
C	ASN228
C	ILE231
C	MG502
C	HOH607
C	HOH623
C	HOH626
C	HOH640
C	HOH656
C	HOH669
C	HOH692
D	LYS252
C	GLY10
C	GLN11
C	ALA12
C	GLN15
C	ASP98
C	ALA99
C	ALA100

site_id	AD3
Number of Residues	5
Details	binding site for residue MG C 502

Chain	Residue
C	GTP501
C	HOH623
C	HOH626
C	HOH640
C	HOH692

site_id	AD4
Number of Residues	3
Details	binding site for residue SO4 C 503

Chain	Residue
C	TYR262
C	ASP431
C	HOH627

site_id	AD5
Number of Residues	4
Details	binding site for residue SO4 C 504

Chain	Residue
C	PRO175
C	LYS394
C	HOH648
D	ASN347

site_id	AD6
Number of Residues	3
Details	binding site for residue SO4 C 505

Chain	Residue
C	ASP211
C	ARG215
C	LYS304

site_id	AD7
Number of Residues	25
Details	binding site for residue GDP D 501

Chain	Residue
D	GLY10
D	GLN11
D	CYS12
D	GLN15
D	SER138
D	GLY141
D	GLY142
D	THR143
D	GLY144
D	PRO171
D	VAL175
D	SER176
D	ASP177
D	GLU181
D	ASN204
D	PHE222
D	ASN226
D	HOH607
D	HOH613
D	HOH624
D	HOH626
D	HOH630
D	HOH638
D	HOH701
D	HOH736

site_id	AD8
Number of Residues	8
Details	binding site for residue SO4 D 502

Chain	Residue
D	THR221
D	ARG276
D	ALA393
D	PHE394
D	HOH610
D	HOH637
D	HOH643
D	HOH710

site_id	AD9
Number of Residues	6
Details	binding site for residue SO4 D 503

Chain	Residue
D	LYS19
D	GLU22
D	HIS227
D	ARG276
D	ARG359
D	HOH661

site_id	AE1
Number of Residues	3
Details	binding site for residue SO4 D 504

Chain	Residue
D	HIS396
D	HOH674
D	HOH740

site_id	AE2
Number of Residues	7
Details	binding site for residue SO4 D 505

Chain	Residue
D	ALA271
D	PRO272
D	LEU273
D	LEU284
D	ASN298
D	HOH691
D	HOH717

site_id	AE3
Number of Residues	4
Details	binding site for residue SO4 E 201

Chain	Residue
E	HIS115
E	ALA118
E	ARG122
E	HOH310

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
A	GLY142-GLY148
B	GLY140-GLY146

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

Chain	Residue	Details
E	ALA73-VAL82

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

Chain	Residue	Details
E	PRO40-GLU49

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

Chain	Residue	Details
B	MET1-ILE4

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	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18327897","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	21
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	99
Details	Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
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)