Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6F1U

N terminal region of dynein tail domains in complex with dynactin filament and BICDR-1

Functional Information from GO Data

Chain	GOid	namespace	contents
c	0005869	cellular_component	dynactin complex
c	0007017	biological_process	microtubule-based process
f	0007018	biological_process	microtubule-based movement
f	0030286	cellular_component	dynein complex
f	0045505	molecular_function	dynein intermediate chain binding
f	0051959	molecular_function	dynein light intermediate chain binding
h	0003777	molecular_function	microtubule motor activity
h	0005515	molecular_function	protein binding
h	0005737	cellular_component	cytoplasm
h	0005813	cellular_component	centrosome
h	0005829	cellular_component	cytosol
h	0005856	cellular_component	cytoskeleton
h	0005868	cellular_component	cytoplasmic dynein complex
h	0005874	cellular_component	microtubule
h	0007018	biological_process	microtubule-based movement
h	0010970	biological_process	transport along microtubule
h	0030286	cellular_component	dynein complex
h	0031982	cellular_component	vesicle
h	0045503	molecular_function	dynein light chain binding
h	0045504	molecular_function	dynein heavy chain binding
K	0003779	molecular_function	actin binding
K	0005737	cellular_component	cytoplasm
K	0005856	cellular_component	cytoskeleton
K	0008290	cellular_component	F-actin capping protein complex
K	0030036	biological_process	actin cytoskeleton organization
K	0030479	cellular_component	actin cortical patch
K	0051015	molecular_function	actin filament binding
K	0051016	biological_process	barbed-end actin filament capping
K	0051693	biological_process	actin filament capping
L	0000902	biological_process	cell morphogenesis
L	0003779	molecular_function	actin binding
L	0005737	cellular_component	cytoplasm
L	0005856	cellular_component	cytoskeleton
L	0007010	biological_process	cytoskeleton organization
L	0008290	cellular_component	F-actin capping protein complex
L	0010591	biological_process	regulation of lamellipodium assembly
L	0022604	biological_process	regulation of cell morphogenesis
L	0030017	cellular_component	sarcomere
L	0030036	biological_process	actin cytoskeleton organization
L	0051015	molecular_function	actin filament binding
L	0051016	biological_process	barbed-end actin filament capping
L	0051490	biological_process	negative regulation of filopodium assembly
L	0051693	biological_process	actin filament capping
L	0071203	cellular_component	WASH complex
m	0007018	biological_process	microtubule-based movement
m	0030286	cellular_component	dynein complex
m	0045505	molecular_function	dynein intermediate chain binding
m	0051959	molecular_function	dynein light intermediate chain binding
n	0007018	biological_process	microtubule-based movement
n	0030286	cellular_component	dynein complex
n	0045505	molecular_function	dynein intermediate chain binding
n	0051959	molecular_function	dynein light intermediate chain binding
x	0005515	molecular_function	protein binding
x	0005737	cellular_component	cytoplasm
x	0005813	cellular_component	centrosome
x	0005856	cellular_component	cytoskeleton
x	0007399	biological_process	nervous system development
x	0031175	biological_process	neuron projection development
x	0031267	molecular_function	small GTPase binding
x	0034452	molecular_function	dynactin binding
x	0047496	biological_process	vesicle transport along microtubule
x	0055107	biological_process	Golgi to secretory granule transport
X	0005515	molecular_function	protein binding
X	0005737	cellular_component	cytoplasm
X	0005813	cellular_component	centrosome
X	0005856	cellular_component	cytoskeleton
X	0007399	biological_process	nervous system development
X	0031175	biological_process	neuron projection development
X	0031267	molecular_function	small GTPase binding
X	0034452	molecular_function	dynactin binding
X	0047496	biological_process	vesicle transport along microtubule
X	0055107	biological_process	Golgi to secretory granule transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue ADP B 800

Chain	Residue
B	ASN16
B	GLY303
B	SER304
B	PHE307
B	GLY17
B	SER18
B	VAL20
B	LYS22
B	GLY161
B	ASP162
B	LYS218
B	GLU219

site_id	AC2
Number of Residues	16
Details	binding site for residue ADP D 800

Chain	Residue
D	GLY17
D	SER18
D	GLY19
D	VAL20
D	LYS22
D	SER160
D	GLY161
D	ASP162
D	LYS218
D	GLU219
D	GLY302
D	GLY303
D	SER304
D	LEU306
D	PHE307
D	LEU337

site_id	AC3
Number of Residues	14
Details	binding site for residue ADP F 800

Chain	Residue
F	GLY17
F	VAL20
F	LYS22
F	SER160
F	GLY161
F	ASP162
F	LYS215
F	LYS218
F	GLU219
F	GLY302
F	GLY303
F	SER304
F	LEU306
F	LEU337

Functional Information from PROSITE/UniProt

site_id	PS00231
Number of Residues	6
Details	F_ACTIN_CAPPING_BETA F-actin capping protein beta subunit signature. CDYNRD

Chain	Residue	Details
L	CYS62-ASP67

site_id	PS00432
Number of Residues	9
Details	ACTINS_2 Actins signature 2. WVSKkEYEE

Chain	Residue	Details
B	TRP357-GLU365

site_id	PS00748
Number of Residues	9
Details	F_ACTIN_CAPPING_A_1 F-actin capping protein alpha subunit signature 1. VHYYEDGNV

Chain	Residue	Details
K	VAL196-VAL204

site_id	PS00749
Number of Residues	11
Details	F_ACTIN_CAPPING_A_2 F-actin capping protein alpha subunit signature 2. KaLRRqLPVTR

Chain	Residue	Details
K	LYS256-ARG266

site_id	PS01132
Number of Residues	13
Details	ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPrkNR

Chain	Residue	Details
B	LEU109-ARG121

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0000250\|UniProtKB:Q13561

Chain	Residue	Details
d	ALA2
m	SER2
n	SER2

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:Q13561

Chain	Residue	Details
d	TYR6
m	SER70
n	SER70

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q62871

Chain	Residue	Details
h	PRO90
m	LYS1125
n	LYS1125

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
h	SER95

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
h	ASP97

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
h	GLY101

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
h	GLY104

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