6ZNL

Cryo-EM structure of the dynactin complex

Functional Information from GO Data

Chain	GOid	namespace	contents
H	0000166	molecular_function	nucleotide binding
H	0001738	biological_process	morphogenesis of a polarized epithelium
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0005856	cellular_component	cytoskeleton
H	0005884	cellular_component	actin filament
H	0005886	cellular_component	plasma membrane
H	0005903	cellular_component	brush border
H	0005911	cellular_component	cell-cell junction
H	0005912	cellular_component	adherens junction
H	0005925	cellular_component	focal adhesion
H	0007017	biological_process	microtubule-based process
H	0007163	biological_process	establishment or maintenance of cell polarity
H	0007409	biological_process	axonogenesis
H	0015629	cellular_component	actin cytoskeleton
H	0016020	cellular_component	membrane
H	0016787	molecular_function	hydrolase activity
H	0016887	molecular_function	ATP hydrolysis activity
H	0019894	molecular_function	kinesin binding
H	0019901	molecular_function	protein kinase binding
H	0030027	cellular_component	lamellipodium
H	0030235	molecular_function	nitric-oxide synthase regulator activity
H	0030424	cellular_component	axon
H	0030863	cellular_component	cortical cytoskeleton
H	0030957	molecular_function	Tat protein binding
H	0032991	cellular_component	protein-containing complex
H	0034333	biological_process	adherens junction assembly
H	0035267	cellular_component	NuA4 histone acetyltransferase complex
H	0036464	cellular_component	cytoplasmic ribonucleoprotein granule
H	0042802	molecular_function	identical protein binding
H	0043296	cellular_component	apical junction complex
H	0044305	cellular_component	calyx of Held
H	0045176	biological_process	apical protein localization
H	0045202	cellular_component	synapse
H	0048870	biological_process	cell motility
H	0050998	molecular_function	nitric-oxide synthase binding
H	0051621	biological_process	regulation of norepinephrine uptake
H	0051726	biological_process	regulation of cell cycle
H	0070160	cellular_component	tight junction
H	0071896	biological_process	protein localization to adherens junction
H	0072749	biological_process	cellular response to cytochalasin B
H	0097433	cellular_component	dense body
H	0098685	cellular_component	Schaffer collateral - CA1 synapse
H	0098871	cellular_component	postsynaptic actin cytoskeleton
H	0098973	molecular_function	structural constituent of postsynaptic actin cytoskeleton
H	0098974	biological_process	postsynaptic actin cytoskeleton organization
H	0098978	cellular_component	glutamatergic synapse
H	0141108	molecular_function	transporter regulator activity
H	0150111	biological_process	regulation of transepithelial transport
H	1900242	biological_process	regulation of synaptic vesicle endocytosis
H	1903076	biological_process	regulation of protein localization to plasma membrane
H	1905168	biological_process	positive regulation of double-strand break repair via homologous recombination
H	1990904	cellular_component	ribonucleoprotein complex
J	0005200	molecular_function	structural constituent of cytoskeleton
J	0005634	cellular_component	nucleus
J	0005856	cellular_component	cytoskeleton
J	0005869	cellular_component	dynactin complex
J	0007010	biological_process	cytoskeleton organization
J	0007017	biological_process	microtubule-based process
J	0098958	biological_process	retrograde axonal transport of mitochondrion
J	1904115	cellular_component	axon cytoplasm
K	0003779	molecular_function	actin binding
K	0005829	cellular_component	cytosol
K	0005856	cellular_component	cytoskeleton
K	0007017	biological_process	microtubule-based process
K	0008290	cellular_component	F-actin capping protein complex
K	0015629	cellular_component	actin cytoskeleton
K	0030036	biological_process	actin cytoskeleton organization
K	0030863	cellular_component	cortical cytoskeleton
K	0051015	molecular_function	actin filament binding
K	0051016	biological_process	barbed-end actin filament capping
K	0051693	biological_process	actin filament capping
L	0003779	molecular_function	actin binding
L	0005737	cellular_component	cytoplasm
L	0005856	cellular_component	cytoskeleton
L	0007017	biological_process	microtubule-based process
L	0008290	cellular_component	F-actin capping protein complex
L	0015629	cellular_component	actin cytoskeleton
L	0030017	cellular_component	sarcomere
L	0030036	biological_process	actin cytoskeleton organization
L	0051016	biological_process	barbed-end actin filament capping
L	0051693	biological_process	actin filament capping
L	0071203	cellular_component	WASH complex
m	0005737	cellular_component	cytoplasm
m	0005813	cellular_component	centrosome
m	0005856	cellular_component	cytoskeleton
m	0005869	cellular_component	dynactin complex
m	0005874	cellular_component	microtubule
m	0007017	biological_process	microtubule-based process
m	0007052	biological_process	mitotic spindle organization
m	0016020	cellular_component	membrane
m	0030286	cellular_component	dynein complex
M	0005737	cellular_component	cytoplasm
M	0005813	cellular_component	centrosome
M	0005856	cellular_component	cytoskeleton
M	0005869	cellular_component	dynactin complex
M	0005874	cellular_component	microtubule
M	0007017	biological_process	microtubule-based process
M	0007052	biological_process	mitotic spindle organization
M	0016020	cellular_component	membrane
M	0030286	cellular_component	dynein complex
n	0005737	cellular_component	cytoplasm
n	0005813	cellular_component	centrosome
n	0005856	cellular_component	cytoskeleton
n	0005869	cellular_component	dynactin complex
n	0005874	cellular_component	microtubule
n	0007017	biological_process	microtubule-based process
n	0007052	biological_process	mitotic spindle organization
n	0016020	cellular_component	membrane
n	0030286	cellular_component	dynein complex
N	0005737	cellular_component	cytoplasm
N	0005813	cellular_component	centrosome
N	0005856	cellular_component	cytoskeleton
N	0005869	cellular_component	dynactin complex
N	0005874	cellular_component	microtubule
N	0007017	biological_process	microtubule-based process
N	0007052	biological_process	mitotic spindle organization
N	0016020	cellular_component	membrane
N	0030286	cellular_component	dynein complex
o	0000776	cellular_component	kinetochore
o	0005737	cellular_component	cytoplasm
o	0005813	cellular_component	centrosome
o	0005819	cellular_component	spindle
o	0005856	cellular_component	cytoskeleton
o	0005869	cellular_component	dynactin complex
o	0007017	biological_process	microtubule-based process
o	0030496	cellular_component	midbody
o	0032154	cellular_component	cleavage furrow
o	0051301	biological_process	cell division
o	0061640	biological_process	cytoskeleton-dependent cytokinesis
O	0000776	cellular_component	kinetochore
O	0005737	cellular_component	cytoplasm
O	0005813	cellular_component	centrosome
O	0005819	cellular_component	spindle
O	0005856	cellular_component	cytoskeleton
O	0005869	cellular_component	dynactin complex
O	0007017	biological_process	microtubule-based process
O	0030496	cellular_component	midbody
O	0032154	cellular_component	cleavage furrow
O	0051301	biological_process	cell division
O	0061640	biological_process	cytoskeleton-dependent cytokinesis
U	0000776	cellular_component	kinetochore
U	0005813	cellular_component	centrosome
U	0005856	cellular_component	cytoskeleton
U	0005869	cellular_component	dynactin complex
U	0007017	biological_process	microtubule-based process
U	0007052	biological_process	mitotic spindle organization
U	0015630	cellular_component	microtubule cytoskeleton
U	0070840	molecular_function	dynein complex binding
V	0000776	cellular_component	kinetochore
V	0005813	cellular_component	centrosome
V	0005856	cellular_component	cytoskeleton
V	0005869	cellular_component	dynactin complex
V	0007017	biological_process	microtubule-based process
Y	0001725	cellular_component	stress fiber
Y	0005813	cellular_component	centrosome
Y	0005856	cellular_component	cytoskeleton
Y	0005869	cellular_component	dynactin complex
Y	0005938	cellular_component	cell cortex
Y	0007017	biological_process	microtubule-based process
Y	0030017	cellular_component	sarcomere

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue ADP A 800

Chain	Residue
A	GLY17
A	GLY302
A	GLY303
A	SER304
A	LEU306
A	LEU337
A	SER18
A	VAL20
A	LYS22
A	GLN142
A	ASP162
A	LYS215
A	LYS218
A	GLU219

---

site_id	AC2
Number of Residues	12
Details	binding site for residue ADP B 800

Chain	Residue
B	GLY17
B	VAL20
B	LYS22
B	GLN142
B	ASP159
B	GLY161
B	ASP162
B	LYS218
B	GLU219
B	GLY303
B	SER304
B	LEU337

---

site_id	AC3
Number of Residues	13
Details	binding site for residue ADP C 800

Chain	Residue
C	GLY17
C	SER18
C	GLY19
C	LYS22
C	GLN142
C	GLY161
C	ASP162
C	LYS218
C	GLU219
C	GLY302
C	GLY303
C	SER304
C	LEU337

---

site_id	AC4
Number of Residues	15
Details	binding site for residue ADP D 800

Chain	Residue
D	ASP15
D	GLY17
D	SER18
D	LYS22
D	GLN142
D	ASP159
D	GLY161
D	ASP162
D	LYS215
D	LYS218
D	GLU219
D	GLY302
D	GLY303
D	SER304
D	LEU337

---

site_id	AC5
Number of Residues	15
Details	binding site for residue ADP E 800

Chain	Residue
E	ASP15
E	GLY17
E	SER18
E	LYS22
E	GLN142
E	ASP159
E	GLY161
E	ASP162
E	LYS218
E	GLU219
E	GLY302
E	GLY303
E	SER304
E	PHE307
E	LEU337

---

site_id	AC6
Number of Residues	9
Details	binding site for residue ADP F 800

Chain	Residue
F	GLY17
F	VAL20
F	LYS22
F	GLN142
F	ASP162
F	LYS218
F	GLU219
F	GLY303
F	SER304

---

site_id	AC7
Number of Residues	11
Details	binding site for residue ADP G 800

Chain	Residue
G	GLY17
G	LYS22
G	ASP159
G	ASP162
G	LYS215
G	LYS218
G	GLU219
G	GLY302
G	GLY303
G	SER304
G	LEU337

---

site_id	AC8
Number of Residues	18
Details	binding site for residue ATP H 401

Chain	Residue
H	LYS213
H	GLU214
H	GLY302
H	THR303
H	MET305
H	TYR306
H	LYS336
H	VAL339
H	ASP11
H	GLY13
H	SER14
H	GLY15
H	MET16
H	LYS18
H	GLN137
H	GLY156
H	ASP157
H	ARG210

---

site_id	AC9
Number of Residues	13
Details	binding site for residue ADP I 800

Chain	Residue
I	GLY17
I	VAL20
I	LYS22
I	GLN142
I	GLY161
I	ASP162
I	LYS218
I	GLU219
I	GLY302
I	GLY303
I	SER304
I	LEU306
I	LEU337

---

site_id	AD1
Number of Residues	16
Details	binding site for residue ADP J 800

Chain	Residue
J	GLY21
J	GLU22
J	ALA23
J	PHE24
J	LYS26
J	GLY142
J	TYR143
J	HIS172
J	GLU208
J	LYS211
J	GLY308
J	THR309
J	MET311
J	ASN351
Y	ARG255
Y	GLN262

---

site_id	AD2
Number of Residues	4
Details	binding site for residue ZN Y 501

Chain	Residue
Y	CYS30
Y	CYS33
Y	ARG37
Y	CYS287

---

site_id	AD3
Number of Residues	4
Details	binding site for residue ZN Y 502

Chain	Residue
Y	CYS51
Y	CYS54
Y	CYS70
Y	CYS73

---

site_id	AD4
Number of Residues	4
Details	binding site for residue ZN Y 503

Chain	Residue
Y	CYS76
Y	CYS79
Y	CYS111
Y	CYS114

---

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	PS00406
Number of Residues	11
Details	ACTINS_1 Actins signature 1. YVGDEAQs.KRG

Chain	Residue	Details
H	TYR53-GLY63

---

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

Chain	Residue	Details
A	TRP357-GLU365
H	TRP356-GLU364

---

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	PS00845
Number of Residues	32
Details	CAP_GLY_1 CAP-Gly domain signature. Gatlfatgk..WvGVilDeak....GKNdGTvqGrkYF

Chain	Residue	Details
Z	GLY48-PHE79

---

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

Chain	Residue	Details
A	LEU109-ARG121
H	LEU104-ARG116

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P60710","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"UniProtKB","id":"P60710","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P60709","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P52907","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52907","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P47756","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P47756","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	81
Details	Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q13561","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q13561","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q13561","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q99KJ8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	24
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"Q13561","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q99KJ8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"O75935","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
Number of Residues	1
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"Q9BTE1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI18
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"Q9UJW0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI19
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9QUR2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI20
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"Q9UJW0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---