Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6W17

Structure of Dip1-activated Arp2/3 complex with nucleated actin filament

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003779	molecular_function	actin binding
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005885	cellular_component	Arp2/3 protein complex
A	0006897	biological_process	endocytosis
A	0015629	cellular_component	actin cytoskeleton
A	0030041	biological_process	actin filament polymerization
A	0030479	cellular_component	actin cortical patch
A	0032153	cellular_component	cell division site
A	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
A	0044396	biological_process	actin cortical patch organization
A	0051015	molecular_function	actin filament binding
A	0051285	cellular_component	cell cortex of cell tip
A	0090135	biological_process	actin filament branching
B	0000147	biological_process	actin cortical patch assembly
B	0000166	molecular_function	nucleotide binding
B	0003779	molecular_function	actin binding
B	0005200	molecular_function	structural constituent of cytoskeleton
B	0005524	molecular_function	ATP binding
B	0005885	cellular_component	Arp2/3 protein complex
B	0005938	cellular_component	cell cortex
B	0006897	biological_process	endocytosis
B	0015629	cellular_component	actin cytoskeleton
B	0030479	cellular_component	actin cortical patch
B	0031097	cellular_component	medial cortex
B	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
B	0051015	molecular_function	actin filament binding
B	0051285	cellular_component	cell cortex of cell tip
B	0090135	biological_process	actin filament branching
C	0000147	biological_process	actin cortical patch assembly
C	0003779	molecular_function	actin binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005885	cellular_component	Arp2/3 protein complex
C	0006897	biological_process	endocytosis
C	0015629	cellular_component	actin cytoskeleton
C	0030036	biological_process	actin cytoskeleton organization
C	0030479	cellular_component	actin cortical patch
C	0030866	biological_process	cortical actin cytoskeleton organization
C	0032153	cellular_component	cell division site
C	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
C	0051015	molecular_function	actin filament binding
C	0051286	cellular_component	cell tip
C	0090135	biological_process	actin filament branching
D	0000147	biological_process	actin cortical patch assembly
D	0003779	molecular_function	actin binding
D	0005200	molecular_function	structural constituent of cytoskeleton
D	0005634	cellular_component	nucleus
D	0005829	cellular_component	cytosol
D	0005885	cellular_component	Arp2/3 protein complex
D	0006897	biological_process	endocytosis
D	0015629	cellular_component	actin cytoskeleton
D	0030041	biological_process	actin filament polymerization
D	0030479	cellular_component	actin cortical patch
D	0032153	cellular_component	cell division site
D	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
D	0051015	molecular_function	actin filament binding
D	0051286	cellular_component	cell tip
D	0090135	biological_process	actin filament branching
E	0000147	biological_process	actin cortical patch assembly
E	0003779	molecular_function	actin binding
E	0005634	cellular_component	nucleus
E	0005826	cellular_component	actomyosin contractile ring
E	0005829	cellular_component	cytosol
E	0005856	cellular_component	cytoskeleton
E	0005885	cellular_component	Arp2/3 protein complex
E	0006897	biological_process	endocytosis
E	0007163	biological_process	establishment or maintenance of cell polarity
E	0015629	cellular_component	actin cytoskeleton
E	0030479	cellular_component	actin cortical patch
E	0030833	biological_process	regulation of actin filament polymerization
E	0032153	cellular_component	cell division site
E	0032432	cellular_component	actin filament bundle
E	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
E	0044396	biological_process	actin cortical patch organization
E	0051015	molecular_function	actin filament binding
E	0051286	cellular_component	cell tip
E	0090135	biological_process	actin filament branching
F	0000147	biological_process	actin cortical patch assembly
F	0003779	molecular_function	actin binding
F	0005634	cellular_component	nucleus
F	0005829	cellular_component	cytosol
F	0005885	cellular_component	Arp2/3 protein complex
F	0006897	biological_process	endocytosis
F	0015629	cellular_component	actin cytoskeleton
F	0030041	biological_process	actin filament polymerization
F	0030479	cellular_component	actin cortical patch
F	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
F	0051015	molecular_function	actin filament binding
F	0090135	biological_process	actin filament branching
G	0000147	biological_process	actin cortical patch assembly
G	0003779	molecular_function	actin binding
G	0005634	cellular_component	nucleus
G	0005829	cellular_component	cytosol
G	0005885	cellular_component	Arp2/3 protein complex
G	0006897	biological_process	endocytosis
G	0015629	cellular_component	actin cytoskeleton
G	0030479	cellular_component	actin cortical patch
G	0030674	molecular_function	protein-macromolecule adaptor activity
G	0030833	biological_process	regulation of actin filament polymerization
G	0030863	cellular_component	cortical cytoskeleton
G	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
G	0043332	cellular_component	mating projection tip
G	0044396	biological_process	actin cortical patch organization
G	0051015	molecular_function	actin filament binding
G	0090135	biological_process	actin filament branching
H	0000147	biological_process	actin cortical patch assembly
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0006897	biological_process	endocytosis
H	0030479	cellular_component	actin cortical patch
H	0032153	cellular_component	cell division site
H	0034314	biological_process	Arp2/3 complex-mediated actin nucleation
H	0043332	cellular_component	mating projection tip
H	0044379	biological_process	protein localization to actin cortical patch
H	0051286	cellular_component	cell tip
H	0051666	biological_process	actin cortical patch localization
H	0071933	molecular_function	Arp2/3 complex binding
I	0000166	molecular_function	nucleotide binding
I	0000287	molecular_function	magnesium ion binding
I	0001725	cellular_component	stress fiber
I	0003785	molecular_function	actin monomer binding
I	0005509	molecular_function	calcium ion binding
I	0005515	molecular_function	protein binding
I	0005523	molecular_function	tropomyosin binding
I	0005524	molecular_function	ATP binding
I	0005737	cellular_component	cytoplasm
I	0005856	cellular_component	cytoskeleton
I	0005865	cellular_component	striated muscle thin filament
I	0005884	cellular_component	actin filament
I	0010628	biological_process	positive regulation of gene expression
I	0016787	molecular_function	hydrolase activity
I	0019904	molecular_function	protein domain specific binding
I	0030027	cellular_component	lamellipodium
I	0030041	biological_process	actin filament polymerization
I	0030175	cellular_component	filopodium
I	0030240	biological_process	skeletal muscle thin filament assembly
I	0031013	molecular_function	troponin I binding
I	0031432	molecular_function	titin binding
I	0031941	cellular_component	filamentous actin
I	0032036	molecular_function	myosin heavy chain binding
I	0032432	cellular_component	actin filament bundle
I	0042802	molecular_function	identical protein binding
I	0044297	cellular_component	cell body
I	0048306	molecular_function	calcium-dependent protein binding
I	0048741	biological_process	skeletal muscle fiber development
I	0051017	biological_process	actin filament bundle assembly
I	0090131	biological_process	mesenchyme migration
I	0098723	cellular_component	skeletal muscle myofibril
I	0140660	molecular_function	cytoskeletal motor activator activity
J	0000166	molecular_function	nucleotide binding
J	0000287	molecular_function	magnesium ion binding
J	0001725	cellular_component	stress fiber
J	0003785	molecular_function	actin monomer binding
J	0005509	molecular_function	calcium ion binding
J	0005515	molecular_function	protein binding
J	0005523	molecular_function	tropomyosin binding
J	0005524	molecular_function	ATP binding
J	0005737	cellular_component	cytoplasm
J	0005856	cellular_component	cytoskeleton
J	0005865	cellular_component	striated muscle thin filament
J	0005884	cellular_component	actin filament
J	0010628	biological_process	positive regulation of gene expression
J	0016787	molecular_function	hydrolase activity
J	0019904	molecular_function	protein domain specific binding
J	0030027	cellular_component	lamellipodium
J	0030041	biological_process	actin filament polymerization
J	0030175	cellular_component	filopodium
J	0030240	biological_process	skeletal muscle thin filament assembly
J	0031013	molecular_function	troponin I binding
J	0031432	molecular_function	titin binding
J	0031941	cellular_component	filamentous actin
J	0032036	molecular_function	myosin heavy chain binding
J	0032432	cellular_component	actin filament bundle
J	0042802	molecular_function	identical protein binding
J	0044297	cellular_component	cell body
J	0048306	molecular_function	calcium-dependent protein binding
J	0048741	biological_process	skeletal muscle fiber development
J	0051017	biological_process	actin filament bundle assembly
J	0090131	biological_process	mesenchyme migration
J	0098723	cellular_component	skeletal muscle myofibril
J	0140660	molecular_function	cytoskeletal motor activator activity
K	0000166	molecular_function	nucleotide binding
K	0000287	molecular_function	magnesium ion binding
K	0001725	cellular_component	stress fiber
K	0003785	molecular_function	actin monomer binding
K	0005509	molecular_function	calcium ion binding
K	0005515	molecular_function	protein binding
K	0005523	molecular_function	tropomyosin binding
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0005856	cellular_component	cytoskeleton
K	0005865	cellular_component	striated muscle thin filament
K	0005884	cellular_component	actin filament
K	0010628	biological_process	positive regulation of gene expression
K	0016787	molecular_function	hydrolase activity
K	0019904	molecular_function	protein domain specific binding
K	0030027	cellular_component	lamellipodium
K	0030041	biological_process	actin filament polymerization
K	0030175	cellular_component	filopodium
K	0030240	biological_process	skeletal muscle thin filament assembly
K	0031013	molecular_function	troponin I binding
K	0031432	molecular_function	titin binding
K	0031941	cellular_component	filamentous actin
K	0032036	molecular_function	myosin heavy chain binding
K	0032432	cellular_component	actin filament bundle
K	0042802	molecular_function	identical protein binding
K	0044297	cellular_component	cell body
K	0048306	molecular_function	calcium-dependent protein binding
K	0048741	biological_process	skeletal muscle fiber development
K	0051017	biological_process	actin filament bundle assembly
K	0090131	biological_process	mesenchyme migration
K	0098723	cellular_component	skeletal muscle myofibril
K	0140660	molecular_function	cytoskeletal motor activator activity
L	0000166	molecular_function	nucleotide binding
L	0000287	molecular_function	magnesium ion binding
L	0001725	cellular_component	stress fiber
L	0003785	molecular_function	actin monomer binding
L	0005509	molecular_function	calcium ion binding
L	0005515	molecular_function	protein binding
L	0005523	molecular_function	tropomyosin binding
L	0005524	molecular_function	ATP binding
L	0005737	cellular_component	cytoplasm
L	0005856	cellular_component	cytoskeleton
L	0005865	cellular_component	striated muscle thin filament
L	0005884	cellular_component	actin filament
L	0010628	biological_process	positive regulation of gene expression
L	0016787	molecular_function	hydrolase activity
L	0019904	molecular_function	protein domain specific binding
L	0030027	cellular_component	lamellipodium
L	0030041	biological_process	actin filament polymerization
L	0030175	cellular_component	filopodium
L	0030240	biological_process	skeletal muscle thin filament assembly
L	0031013	molecular_function	troponin I binding
L	0031432	molecular_function	titin binding
L	0031941	cellular_component	filamentous actin
L	0032036	molecular_function	myosin heavy chain binding
L	0032432	cellular_component	actin filament bundle
L	0042802	molecular_function	identical protein binding
L	0044297	cellular_component	cell body
L	0048306	molecular_function	calcium-dependent protein binding
L	0048741	biological_process	skeletal muscle fiber development
L	0051017	biological_process	actin filament bundle assembly
L	0090131	biological_process	mesenchyme migration
L	0098723	cellular_component	skeletal muscle myofibril
L	0140660	molecular_function	cytoskeletal motor activator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	binding site for residue MG A 500

Chain	Residue
A	ATP501

site_id	AC2
Number of Residues	13
Details	binding site for residue ATP A 501

Chain	Residue
A	GLU242
A	GLY335
A	SER336
A	LEU338
A	MG500
A	GLY13
A	THR14
A	GLY15
A	TYR16
A	LYS18
A	GLY187
A	ASP188
A	LYS241

site_id	AC3
Number of Residues	3
Details	binding site for residue MG B 500

Chain	Residue
B	GLN137
B	ASP154
B	ATP501

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

Chain	Residue
B	GLY11
B	THR12
B	PHE14
B	GLN137
B	GLY156
B	ASP157
B	ARG210
B	LYS213
B	GLU214
B	GLY302
B	ARG347
B	MG500

site_id	AC5
Number of Residues	13
Details	binding site for residue ADP I 401

Chain	Residue
I	ASP11
I	GLY13
I	LEU16
I	LYS18
I	GLY156
I	ASP157
I	LYS213
I	GLU214
I	GLY301
I	GLY302
I	THR303
I	LYS336
I	MG402

site_id	AC6
Number of Residues	4
Details	binding site for residue MG I 402

Chain	Residue
I	GLN137
I	ASP154
I	GLY156
I	ADP401

site_id	AC7
Number of Residues	10
Details	binding site for residue ADP J 401

Chain	Residue
J	GLY13
J	LYS18
J	GLN137
J	GLY156
J	ASP157
J	LYS213
J	GLU214
J	GLY302
J	THR303
J	MG402

site_id	AC8
Number of Residues	4
Details	binding site for residue MG J 402

Chain	Residue
J	GLN137
J	ASP154
J	GLY156
J	ADP401

site_id	AC9
Number of Residues	13
Details	binding site for residue ADP K 401

Chain	Residue
K	GLY13
K	LEU16
K	LYS18
K	GLY156
K	ASP157
K	LYS213
K	GLU214
K	GLY301
K	GLY302
K	THR303
K	MET305
K	LYS336
K	MG402

site_id	AD1
Number of Residues	2
Details	binding site for residue MG K 402

Chain	Residue
K	GLY156
K	ADP401

site_id	AD2
Number of Residues	13
Details	binding site for residue ADP L 401

Chain	Residue
L	GLY13
L	LYS18
L	GLN137
L	GLY156
L	ASP157
L	ARG210
L	LYS213
L	GLU214
L	GLY302
L	THR303
L	TYR306
L	LYS336
L	MG402

site_id	AD3
Number of Residues	3
Details	binding site for residue MG L 402

Chain	Residue
L	GLN137
L	GLY156
L	ADP401

site_id	AD4
Number of Residues	4
Details	binding site for Di-peptide HYP X 1 and CYS X 7

Chain	Residue
B	ASP179
M	ALA2
M	TRP3
M	ALO6

site_id	AD5
Number of Residues	5
Details	binding site for Di-peptide HYP X 1 and ALA X 2

Chain	Residue
M	CYS7
B	GLU72
B	ILE75
M	TRP3
M	G5G4

site_id	AD6
Number of Residues	8
Details	binding site for Di-peptide TRP X 3 and G5G X 4

Chain	Residue
B	ARG177
I	GLY197
I	GLN246
M	HYP1
M	ALA2
M	ALA5
M	ALO6
M	CYS7

site_id	AD7
Number of Residues	4
Details	binding site for Di-peptide G5G X 4 and ALA X 5

Chain	Residue
I	GLN246
M	ALA2
M	TRP3
M	ALO6

site_id	AD8
Number of Residues	6
Details	binding site for Di-peptide ALA X 5 and ALO X 6

Chain	Residue
I	SER199
I	GLU205
I	GLN246
M	TRP3
M	G5G4
M	CYS7

site_id	AD9
Number of Residues	7
Details	binding site for Di-peptide ALO X 6 and CYS X 7

Chain	Residue
B	ASP179
I	SER199
I	GLU205
M	HYP1
M	ALA2
M	TRP3
M	ALA5

site_id	AE1
Number of Residues	4
Details	binding site for Di-peptide HYP Y 1 and CYS Y 7

Chain	Residue
J	ASP179
O	ALA2
O	TRP3
O	ALO6

site_id	AE2
Number of Residues	3
Details	binding site for Di-peptide HYP Y 1 and ALA Y 2

Chain	Residue
O	TRP3
O	G5G4
O	CYS7

site_id	AE3
Number of Residues	8
Details	binding site for Di-peptide TRP Y 3 and G5G Y 4

Chain	Residue
J	ILE75
J	ARG177
K	GLY197
O	HYP1
O	ALA2
O	ALA5
O	ALO6
O	CYS7

site_id	AE4
Number of Residues	5
Details	binding site for Di-peptide G5G Y 4 and ALA Y 5

Chain	Residue
K	GLY197
K	GLN246
O	ALA2
O	TRP3
O	ALO6

site_id	AE5
Number of Residues	5
Details	binding site for Di-peptide ALA Y 5 and ALO Y 6

Chain	Residue
K	SER199
K	GLN246
O	TRP3
O	G5G4
O	CYS7

site_id	AE6
Number of Residues	6
Details	binding site for Di-peptide ALO Y 6 and CYS Y 7

Chain	Residue
J	ASP179
K	SER199
O	HYP1
O	ALA2
O	TRP3
O	ALA5

site_id	AE7
Number of Residues	5
Details	binding site for Di-peptide HYP Z 1 and CYS Z 7

Chain	Residue
I	ASP179
J	SER199
N	ALA2
N	TRP3
N	ALO6

site_id	AE8
Number of Residues	4
Details	binding site for Di-peptide HYP Z 1 and ALA Z 2

Chain	Residue
I	ILE75
N	TRP3
N	G5G4
N	CYS7

site_id	AE9
Number of Residues	7
Details	binding site for Di-peptide TRP Z 3 and G5G Z 4

Chain	Residue
I	ARG177
J	GLY197
N	HYP1
N	ALA2
N	ALA5
N	ALO6
N	CYS7

site_id	AF1
Number of Residues	6
Details	binding site for Di-peptide G5G Z 4 and ALA Z 5

Chain	Residue
B	ARG290
J	TYR198
J	GLN246
N	ALA2
N	TRP3
N	ALO6

site_id	AF2
Number of Residues	9
Details	binding site for Di-peptide ALA Z 5 and ALO Z 6

Chain	Residue
B	ARG290
J	TYR198
J	SER199
J	PHE200
J	GLU205
J	GLN246
N	TRP3
N	G5G4
N	CYS7

site_id	AF3
Number of Residues	8
Details	binding site for Di-peptide ALO Z 6 and CYS Z 7

Chain	Residue
I	ASP179
J	SER199
J	PHE200
J	GLU205
N	HYP1
N	ALA2
N	TRP3
N	ALA5

site_id	AF4
Number of Residues	6
Details	binding site for Di-peptide HYP a 1 and CYS a 7

Chain	Residue
L	GLU72
L	HIC73
L	ASP179
Q	ALA2
Q	TRP3
Q	ALO6

site_id	AF5
Number of Residues	6
Details	binding site for Di-peptide HYP a 1 and ALA a 2

Chain	Residue
L	GLU72
L	HIC73
L	ILE75
Q	TRP3
Q	G5G4
Q	CYS7

site_id	AF6
Number of Residues	8
Details	binding site for Di-peptide TRP a 3 and G5G a 4

Chain	Residue
L	ILE75
L	ARG177
L	ASP179
Q	HYP1
Q	ALA2
Q	ALA5
Q	ALO6
Q	CYS7

site_id	AF7
Number of Residues	3
Details	binding site for Di-peptide G5G a 4 and ALA a 5

Chain	Residue
Q	ALA2
Q	TRP3
Q	ALO6

site_id	AF8
Number of Residues	3
Details	binding site for Di-peptide ALA a 5 and ALO a 6

Chain	Residue
Q	TRP3
Q	G5G4
Q	CYS7

site_id	AF9
Number of Residues	6
Details	binding site for Di-peptide ALO a 6 and CYS a 7

Chain	Residue
L	HIC73
L	ASP179
Q	HYP1
Q	ALA2
Q	TRP3
Q	ALA5

site_id	AG1
Number of Residues	5
Details	binding site for Di-peptide HYP b 1 and ALA b 2

Chain	Residue
K	GLU72
K	ILE75
P	TRP3
P	G5G4
P	CYS7

site_id	AG2
Number of Residues	5
Details	binding site for Di-peptide HYP b 1 and CYS b 7

Chain	Residue
K	GLU72
K	ASP179
P	ALA2
P	TRP3
P	ALO6

site_id	AG3
Number of Residues	10
Details	binding site for Di-peptide TRP b 3 and G5G b 4

Chain	Residue
K	ILE75
K	ARG177
L	GLY197
L	TYR198
L	GLN246
P	HYP1
P	ALA2
P	ALA5
P	ALO6
P	CYS7

site_id	AG4
Number of Residues	5
Details	binding site for Di-peptide G5G b 4 and ALA b 5

Chain	Residue
L	GLY197
L	GLN246
P	ALA2
P	TRP3
P	ALO6

site_id	AG5
Number of Residues	6
Details	binding site for Di-peptide ALA b 5 and ALO b 6

Chain	Residue
L	SER199
L	PHE200
L	GLU205
P	TRP3
P	G5G4
P	CYS7

site_id	AG6
Number of Residues	8
Details	binding site for Di-peptide ALO b 6 and CYS b 7

Chain	Residue
K	ASP179
L	SER199
L	PHE200
L	GLU205
P	HYP1
P	ALA2
P	TRP3
P	ALA5

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
I	TYR53-GLY63

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

Chain	Residue	Details
I	TRP356-GLU364

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

Chain	Residue	Details
I	LEU104-ARG116
A	LEU127-ARG139
B	LEU104-ARG116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	11
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	39
Details	Repeat: {"description":"WD 1"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	39
Details	Repeat: {"description":"WD 2"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	41
Details	Repeat: {"description":"WD 3"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	39
Details	Repeat: {"description":"WD 4"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	39
Details	Repeat: {"description":"WD 5"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	34
Details	Repeat: {"description":"WD 6"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	100
Details	Region: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	8
Details	Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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