Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8JJB

Crystal structure of T2R-TTL-Y61 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	0005737	cellular_component	cytoplasm
E	0005794	cellular_component	Golgi apparatus
E	0007019	biological_process	microtubule depolymerization
E	0015631	molecular_function	tubulin binding
E	0030424	cellular_component	axon
E	0030426	cellular_component	growth cone
E	0031110	biological_process	regulation of microtubule polymerization or depolymerization
E	0031175	biological_process	neuron projection development
E	0042995	cellular_component	cell projection
E	0043005	cellular_component	neuron projection
F	0000226	biological_process	microtubule cytoskeleton organization
F	0004835	molecular_function	tubulin-tyrosine ligase activity
F	0005876	cellular_component	spindle microtubule
F	0016874	molecular_function	ligase activity
F	0036211	biological_process	protein modification process
F	0043687	biological_process	post-translational protein modification
F	0045931	biological_process	positive regulation of mitotic cell cycle
F	0046872	molecular_function	metal ion binding
F	0090235	biological_process	regulation of metaphase plate congression

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	GLY140-GLY146
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	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:22673903

Chain	Residue	Details
E	SER46
D	GLY142
D	THR143
D	GLY144
D	ASN204
D	ASN226
B	SER138
B	GLY142
B	THR143
B	GLY144
B	ASN204
B	ASN226
D	GLN11
D	SER138

site_id	SWS_FT_FI2
Number of Residues	2
Details	LIPID: S-palmitoyl cysteine => ECO:0000250

Chain	Residue	Details
E	CYS-24
C	GLU71
C	SER140
C	GLY144
C	THR145
C	THR179
C	ASN206
C	ASN228
E	CYS-22
A	SER140
A	GLY144
A	THR145
A	THR179
A	ASN206
A	ASN228
C	GLN11

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P99024

Chain	Residue	Details
B	SER40
D	SER40

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P99024

Chain	Residue	Details
B	LYS58
D	LYS58

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine; by CDK1 => ECO:0000250\|UniProtKB:Q13885

Chain	Residue	Details
B	SER172
D	SER172
C	SER48
C	SER232

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P07437

Chain	Residue	Details
B	THR285
B	THR290
D	THR285
D	THR290

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250\|UniProtKB:P07437

Chain	Residue	Details
B	ARG318
D	ARG318

site_id	SWS_FT_FI8
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250\|UniProtKB:P07437

Chain	Residue	Details
B	LYS58
D	LYS58

site_id	SWS_FT_FI9
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:P07437

Chain	Residue	Details
A	GLU443
B	LYS324
D	LYS324

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: 5-glutamyl polyglutamate => ECO:0000250\|UniProtKB:P68369

Chain	Residue	Details
A	GLU445
C	GLU445

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: 3'-nitrotyrosine => ECO:0000250\|UniProtKB:Q71U36

Chain	Residue	Details
A	TYR451
C	TYR451

site_id	SWS_FT_FI12
Number of Residues	6
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	LYS326
A	LYS370
C	LYS326
C	LYS370

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