Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6REV

Cryo-EM structure of the N-terminal DC repeat (NDC) of human doublecortin (DCX) bound to 13-protofilament GDP-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	0003725	molecular_function	double-stranded RNA binding
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	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005874	cellular_component	microtubule
A	0005881	cellular_component	cytoplasmic microtubule
A	0005929	cellular_component	cilium
A	0007017	biological_process	microtubule-based process
A	0015630	cellular_component	microtubule cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0046872	molecular_function	metal ion binding
A	0071353	biological_process	cellular response to interleukin-4
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
N	0035556	biological_process	intracellular signal transduction
a	0000166	molecular_function	nucleotide binding
a	0000226	biological_process	microtubule cytoskeleton organization
a	0000278	biological_process	mitotic cell cycle
a	0003725	molecular_function	double-stranded RNA binding
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	0005829	cellular_component	cytosol
a	0005856	cellular_component	cytoskeleton
a	0005874	cellular_component	microtubule
a	0005881	cellular_component	cytoplasmic microtubule
a	0005929	cellular_component	cilium
a	0007017	biological_process	microtubule-based process
a	0015630	cellular_component	microtubule cytoskeleton
a	0016787	molecular_function	hydrolase activity
a	0031625	molecular_function	ubiquitin protein ligase binding
a	0046872	molecular_function	metal ion binding
a	0071353	biological_process	cellular response to interleukin-4
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue GDP b 501

Chain	Residue
a	LEU248
b	ASN204
b	TYR222
b	ASN226
b	GLN11
b	CYS12
b	GLN15
b	GLY141
b	GLY142
b	THR143
b	GLY144
b	ASP177

site_id	AC2
Number of Residues	17
Details	binding site for residue GTP A 501

Chain	Residue
A	GLY10
A	GLN11
A	ALA12
A	GLN15
A	GLU71
A	ASP98
A	SER140
A	GLY143
A	GLY144
A	THR145
A	ILE171
A	THR179
A	ASN206
A	TYR224
A	ASN228
A	ILE231
A	MG502

site_id	AC3
Number of Residues	2
Details	binding site for residue MG A 502

Chain	Residue
A	GLN11
A	GTP501

site_id	AC4
Number of Residues	12
Details	binding site for residue GDP B 501

Chain	Residue
A	LEU248
B	GLN11
B	CYS12
B	GLN15
B	GLY141
B	GLY142
B	THR143
B	GLY144
B	ASP177
B	ASN204
B	TYR222
B	ASN226

site_id	AC5
Number of Residues	17
Details	binding site for residue GTP a 501

Chain	Residue
a	GLY10
a	GLN11
a	ALA12
a	GLN15
a	GLU71
a	ASP98
a	SER140
a	GLY143
a	GLY144
a	THR145
a	ILE171
a	THR179
a	ASN206
a	TYR224
a	ASN228
a	ILE231
a	MG502

site_id	AC6
Number of Residues	2
Details	binding site for residue MG a 502

Chain	Residue
a	GLN11
a	GTP501

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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	86
Details	Domain: {"description":"Doublecortin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00072","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by MARK1 and PKA","evidences":[{"source":"UniProtKB","id":"Q9ESI7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by ABL","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by CK2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by CK2, MARK1 and PKA","evidences":[{"source":"UniProtKB","id":"Q9ESI7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Motif: {"description":"MREI motif","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q3KRE8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
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_FI13
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"UniProtKB","id":"Q9BVA1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
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_FI16
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_FI17
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_FI18
Number of Residues	2
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
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_FI21
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_FI22
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
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

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