Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5XKG

Crystal structure of T2R-TTL-CH1 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	28
Details	binding site for residue GTP A 501

Chain	Residue
A	GLY10
A	GLY144
A	THR145
A	GLY146
A	VAL177
A	THR179
A	GLU183
A	ASN206
A	TYR224
A	ASN228
A	ILE231
A	GLN11
A	MG502
A	HOH626
A	HOH638
A	HOH650
A	HOH655
A	HOH664
A	HOH668
A	HOH709
A	HOH712
A	ALA12
A	GLN15
A	ASP98
A	ALA99
A	ASN101
A	SER140
A	GLY143

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

Chain	Residue
A	GTP501
A	HOH638
A	HOH650
A	HOH664
A	HOH709

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	HOH659

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

Chain	Residue
A	ASN216
A	PRO274
A	VAL275
A	ILE276
A	ASN300
A	HOH673
A	HOH681

site_id	AC5
Number of Residues	21
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	VAL175
B	ASP177
B	GLU181
B	ASN204
B	TYR222
B	ASN226
B	MG502
B	HOH608
B	HOH612
B	HOH625
B	HOH655
B	HOH688

site_id	AC6
Number of Residues	6
Details	binding site for residue MG B 502

Chain	Residue
B	GLN11
B	GDP501
B	HOH609
B	HOH662
B	HOH688
C	HOH769

site_id	AC7
Number of Residues	9
Details	binding site for residue MES B 503

Chain	Residue
B	ARG156
B	ASP161
B	ARG162
B	ASN195
B	ASP197
B	ARG251
B	HOH673
B	HOH674
B	HOH698

site_id	AC8
Number of Residues	16
Details	binding site for residue 890 B 504

Chain	Residue
A	THR179
A	ALA180
A	VAL181
B	CYS239
B	LEU240
B	LEU246
B	ALA248
B	LYS252
B	LEU253
B	ASN256
B	MET257
B	ALA315
B	ILE316
B	ASN348
B	LYS350
B	ALA352

site_id	AC9
Number of Residues	27
Details	binding site for residue GTP C 501

Chain	Residue
C	ALA12
C	GLN15
C	ASP98
C	ALA99
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	HOH617
C	HOH638
C	HOH652
C	HOH674
C	HOH676
C	HOH766
D	LYS252
C	GLY10
C	GLN11

site_id	AD1
Number of Residues	5
Details	binding site for residue MG C 502

Chain	Residue
C	GTP501
C	HOH612
C	HOH617
C	HOH652
C	HOH766

site_id	AD2
Number of Residues	5
Details	binding site for residue CA C 503

Chain	Residue
C	ASP39
C	THR41
C	GLY44
C	GLU55
C	HOH618

site_id	AD3
Number of Residues	19
Details	binding site for residue GTP D 501

Chain	Residue
D	GLY10
D	GLN11
D	CYS12
D	GLN15
D	ALA97
D	GLY98
D	ASN99
D	SER138
D	GLY141
D	GLY142
D	THR143
D	GLY144
D	VAL175
D	GLU181
D	ASN204
D	TYR222
D	ASN226
D	MG502
D	HOH616

site_id	AD4
Number of Residues	2
Details	binding site for residue MG D 502

Chain	Residue
D	GLN11
D	GTP501

site_id	AD5
Number of Residues	13
Details	binding site for residue 890 D 503

Chain	Residue
C	THR179
C	ALA180
C	VAL181
D	CYS239
D	ALA248
D	LYS252
D	LEU253
D	ASN256
D	MET257
D	ALA315
D	ILE316
D	ASN348
D	LYS350

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	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	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_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	6
Details	Motif: {"description":"MREI motif","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":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
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_FI21
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_FI22
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
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_FI24
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_FI25
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_FI26
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)