Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3JAW

Atomic model of a microtubule seam based on a cryo-EM reconstruction of the EB3-bound microtubule (merged dataset containing tubulin bound to GTPgammaS, GMPCPP, and GDP)

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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	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	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	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	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GTP A 501

Chain	Residue
A	GLY10
A	GLY143
A	GLY144
A	THR145
A	GLY146
A	THR179
A	GLU183
A	ASN206
A	TYR224
A	ASN228
A	MG502
A	GLN11
B	LEU248
B	LYS254
A	ALA12
A	GLN15
A	ASP98
A	ALA99
A	ALA100
A	ASN101
A	SER140

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 502

Chain	Residue
A	GLU71
A	GTP501
B	LYS254

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GSP B 501

Chain	Residue
B	GLN11
B	CYS12
B	GLN15
B	GLU71
B	ALA99
B	ASN101
B	SER140
B	GLY143
B	GLY144
B	THR145
B	GLY146
B	ASP179
B	ASN206
B	TYR224
B	ASN228

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE GTP C 501

Chain	Residue
C	GLY10
C	GLN11
C	ALA12
C	GLN15
C	ALA99
C	ASN101
C	SER140
C	GLY143
C	GLY144
C	THR145
C	GLY146
C	THR179
C	GLU183
C	ASN206
C	TYR224
C	ASN228
C	MG502

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG C 502

Chain	Residue
C	GLU71
C	GTP501

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GSP D 501

Chain	Residue
C	GLU254
D	GLY10
D	GLN11
D	CYS12
D	GLU71
D	SER140
D	GLY143
D	GLY144
D	THR145
D	GLY146
D	ASP179
D	ASN206
D	ASN228

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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q13509

Chain	Residue	Details
B	GLN11
D	GLY144
D	THR145
D	GLY146
D	ASN206
D	ASN228
B	SER140
B	GLY144
B	THR145
B	GLY146
B	ASN206
B	ASN228
D	GLN11
D	SER140

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
B	GLU71
C	GLU71
C	SER140
C	GLY144
C	THR145
C	THR179
C	ASN206
C	ASN228
D	GLU71
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	LYS60
D	LYS60

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

Chain	Residue	Details
B	SER174
D	SER174
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	THR287
B	THR292
D	THR287
D	THR292

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

Chain	Residue	Details
B	ARG320
D	ARG320

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: 5-glutamyl polyglutamate => ECO:0000250\|UniProtKB:Q2T9S0

Chain	Residue	Details
B	GLU448
D	GLU448

site_id	SWS_FT_FI9
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	LYS60
D	LYS60

site_id	SWS_FT_FI10
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	GLU445
B	LYS326
D	LYS326

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)