Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2P4N

Human Monomeric Kinesin (1BG2) and Bovine Tubulin (1JFF) Docked into the 9-Angstrom Cryo-EM Map of Nucleotide-Free Kinesin Complexed to the 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	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	0005929	cellular_component	cilium
A	0007017	biological_process	microtubule-based process
A	0016787	molecular_function	hydrolase activity
A	0031514	cellular_component	motile cilium
A	0042995	cellular_component	cell projection
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	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	0007399	biological_process	nervous system development
B	0015630	cellular_component	microtubule cytoskeleton
B	0046872	molecular_function	metal ion binding
B	0046982	molecular_function	protein heterodimerization activity
B	1902669	biological_process	positive regulation of axon guidance
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	2
Details	BINDING SITE FOR RESIDUE MG K 402

Chain	Residue
K	THR92
K	ADP401

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ZN A 900

Chain	Residue
A	HIS283

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 501

Chain	Residue
A	GLN11
A	GLU71
B	GTP500

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ADP K 401

Chain	Residue
K	GLN86
K	THR87
K	SER88
K	SER89
K	GLY90
K	LYS91
K	THR92
K	HIS93
K	MG402
K	ARG14
K	ARG16
K	PRO17

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE GTP B 500

Chain	Residue
A	GLY10
A	GLN11
A	ALA12
A	GLN15
A	ALA99
A	ALA100
A	ASN101
A	SER140
A	GLY143
A	GLY144
A	THR145
A	GLY146
A	ILE171
A	GLU183
A	ASN206
A	TYR224
A	ASN228
A	MG501
B	LEU248
B	LYS254

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GDP B 600

Chain	Residue
B	GLY10
B	GLN11
B	CYS12
B	GLN15
B	SER140
B	GLY142
B	GLY144
B	THR145
B	GLY146
B	ASP179
B	ASN206
B	TYR224
B	ASN228

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TA1 B 601

Chain	Residue
B	VAL23
B	ASP26
B	GLU27
B	HIS229
B	LEU230
B	ALA233
B	SER236
B	PHE272
B	PRO274
B	LEU275
B	THR276
B	ARG278
B	PRO360
B	ARG369
B	GLY370

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	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. GKLyLVDLAGSE

Chain	Residue	Details
K	GLY225-GLU236

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	317
Details	Domain: {"description":"Kinesin motor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00283","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	7
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
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	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q3KRE8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"UniProtKB","id":"Q9BVA1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	1
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
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_FI16
Number of Residues	2
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

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1goj

Chain	Residue	Details
K	GLY234

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