Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6B0C

KLP10A-AMPPNP in complex with curved tubulin and 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	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
K	0003777	molecular_function	microtubule motor activity
K	0005524	molecular_function	ATP binding
K	0007018	biological_process	microtubule-based movement
K	0008017	molecular_function	microtubule binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue GTP A 501

Chain	Residue
A	GLN11
A	GLY144
A	THR145
A	PRO173
A	THR179
A	ASN206
A	TYR224
A	ASN228
A	MG502
B	LYS252
A	ALA12
A	GLN15
A	GLU71
A	ALA99
A	ALA100
A	ASN101
A	SER140
A	GLY143

site_id	AC2
Number of Residues	3
Details	binding site for residue MG A 502

Chain	Residue
A	GLU71
A	GTP501
B	LYS252

site_id	AC3
Number of Residues	15
Details	binding site for residue GDP B 501

Chain	Residue
B	GLN11
B	CYS12
B	GLN15
B	GLU69
B	ALA97
B	ASN99
B	SER138
B	GLY141
B	GLY142
B	THR143
B	GLY144
B	GLU181
B	ASN204
B	TYR222
B	ASN226

site_id	AC4
Number of Residues	22
Details	binding site for residue GTP C 501

Chain	Residue
C	GLY10
C	GLN11
C	ALA12
C	GLN15
C	ASP98
C	ALA99
C	ALA100
C	ASN101
C	SER140
C	GLY142
C	GLY143
C	GLY144
C	THR145
C	GLY146
C	ILE171
C	THR179
C	ASN206
C	TYR224
C	ASN228
C	MG502
D	LEU246
D	LYS252

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	14
Details	binding site for residue GDP D 501

Chain	Residue
D	GLY10
D	GLN11
D	CYS12
D	GLN15
D	ASN99
D	SER138
D	GLY141
D	GLY142
D	THR143
D	GLY144
D	ASP177
D	ASN204
D	TYR222
D	ASN226

site_id	AC7
Number of Residues	13
Details	binding site for residue TA1 D 502

Chain	Residue
D	VAL23
D	GLU27
D	LEU215
D	ASP224
D	HIS227
D	ALA231
D	PRO272
D	LEU273
D	THR274
D	ARG276
D	PRO358
D	ARG359
D	LEU361

site_id	AC8
Number of Residues	3
Details	binding site for residue MG K 701

Chain	Residue
K	THR375
K	SER488
K	ANP702

site_id	AC9
Number of Residues	15
Details	binding site for residue ANP K 702

Chain	Residue
K	HIS376
K	PHE382
K	SER487
K	SER488
K	ALA516
K	MG701
K	ARG284
K	PRO287
K	GLN369
K	THR370
K	GLY371
K	SER372
K	GLY373
K	LYS374
K	THR375

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

Chain	Residue	Details
K	GLY508-GLU519

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	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
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_FI10
Number of Residues	6
Details	Motif: {"description":"MREI motif","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
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_FI14
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_FI15
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
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_FI17
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_FI18
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_FI19
Number of Residues	332
Details	Domain: {"description":"Kinesin motor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00283","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00283","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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