Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8UTT

KIF1A[1-393] P305L mutant AMP-PNP bound two-heads-bound state in complex with a microtubule

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	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	0007010	biological_process	cytoskeleton organization
B	0007017	biological_process	microtubule-based process
B	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0000226	biological_process	microtubule cytoskeleton organization
E	0000278	biological_process	mitotic cell cycle
E	0003924	molecular_function	GTPase activity
E	0005200	molecular_function	structural constituent of cytoskeleton
E	0005525	molecular_function	GTP binding
E	0005737	cellular_component	cytoplasm
E	0005856	cellular_component	cytoskeleton
E	0005874	cellular_component	microtubule
E	0007017	biological_process	microtubule-based process
E	0015630	cellular_component	microtubule cytoskeleton
E	0016787	molecular_function	hydrolase activity
E	0046872	molecular_function	metal ion binding
I	0000166	molecular_function	nucleotide binding
I	0003924	molecular_function	GTPase activity
I	0005200	molecular_function	structural constituent of cytoskeleton
I	0005525	molecular_function	GTP binding
I	0005737	cellular_component	cytoplasm
I	0005856	cellular_component	cytoskeleton
I	0005874	cellular_component	microtubule
I	0007010	biological_process	cytoskeleton organization
I	0007017	biological_process	microtubule-based process
I	0046872	molecular_function	metal ion binding
K	0003700	molecular_function	DNA-binding transcription factor activity
K	0003777	molecular_function	microtubule motor activity
K	0005524	molecular_function	ATP binding
K	0006355	biological_process	regulation of DNA-templated transcription
K	0007018	biological_process	microtubule-based movement
K	0008017	molecular_function	microtubule binding
N	0003700	molecular_function	DNA-binding transcription factor activity
N	0003777	molecular_function	microtubule motor activity
N	0005524	molecular_function	ATP binding
N	0006355	biological_process	regulation of DNA-templated transcription
N	0007018	biological_process	microtubule-based movement
N	0008017	molecular_function	microtubule binding
S	0000166	molecular_function	nucleotide binding
S	0000226	biological_process	microtubule cytoskeleton organization
S	0000278	biological_process	mitotic cell cycle
S	0003924	molecular_function	GTPase activity
S	0005200	molecular_function	structural constituent of cytoskeleton
S	0005525	molecular_function	GTP binding
S	0005737	cellular_component	cytoplasm
S	0005856	cellular_component	cytoskeleton
S	0005874	cellular_component	microtubule
S	0007017	biological_process	microtubule-based process
S	0015630	cellular_component	microtubule cytoskeleton
S	0016787	molecular_function	hydrolase activity
S	0046872	molecular_function	metal ion binding

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	PS00411
Number of Residues	12
Details	KINESIN_MOTOR_1 Kinesin motor domain signature. SKIsLVDLAGSE

Chain	Residue	Details
K	SER242-GLU253

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: ACT_SITE => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	GLU254
N	SER215
E	GLU254
S	GLU254
K	TYR105
K	SER215
N	GLY102
N	LYS103
N	SER104
N	TYR105

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	GLN11
E	GLU71
E	SER140
E	GLY144
E	THR145
E	THR179
E	ASN206
E	ASN228
S	GLN11
S	GLU71
S	SER140
A	GLU71
S	GLY144
S	THR145
S	THR179
S	ASN206
S	ASN228
A	SER140
A	GLY144
A	THR145
A	THR179
A	ASN206
A	ASN228
E	GLN11

site_id	SWS_FT_FI3
Number of Residues	3
Details	SITE: Involved in polymerization => ECO:0000250

Chain	Residue	Details
A	TYR451
E	TYR451
S	TYR451

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	LYS40
E	LYS40
S	LYS40

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	SER48
A	SER232
E	SER48
E	SER232
S	SER48
S	SER232

site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: 3'-nitrotyrosine => ECO:0000250\|UniProtKB:P68373

Chain	Residue	Details
A	TYR282
E	TYR282
S	TYR282

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	ARG339
E	ARG339
S	ARG339

site_id	SWS_FT_FI8
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P68373

Chain	Residue	Details
A	SER439
E	SER439
S	SER439

site_id	SWS_FT_FI9
Number of Residues	3
Details	MOD_RES: 5-glutamyl polyglutamate => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	GLU443
E	GLU443
S	GLU443

site_id	SWS_FT_FI10
Number of Residues	3
Details	MOD_RES: 5-glutamyl polyglutamate => ECO:0000250\|UniProtKB:P68369

Chain	Residue	Details
A	GLU445
E	GLU445
S	GLU445

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

Chain	Residue	Details
A	TYR451
E	TYR451
S	TYR451

site_id	SWS_FT_FI12
Number of Residues	9
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:P68363

Chain	Residue	Details
A	LYS326
A	LYS370
E	LYS326
E	LYS370
S	LYS326
S	LYS370

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)