Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6GVC

Structure of ArhGAP12 bound to G-Actin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0001725	cellular_component	stress fiber
A	0003785	molecular_function	actin monomer binding
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005523	molecular_function	tropomyosin binding
A	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0005865	cellular_component	striated muscle thin filament
A	0005884	cellular_component	actin filament
A	0010628	biological_process	positive regulation of gene expression
A	0016887	molecular_function	ATP hydrolysis activity
A	0019904	molecular_function	protein domain specific binding
A	0030027	cellular_component	lamellipodium
A	0030041	biological_process	actin filament polymerization
A	0030175	cellular_component	filopodium
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0031013	molecular_function	troponin I binding
A	0031432	molecular_function	titin binding
A	0031941	cellular_component	filamentous actin
A	0032036	molecular_function	myosin heavy chain binding
A	0032432	cellular_component	actin filament bundle
A	0042802	molecular_function	identical protein binding
A	0044297	cellular_component	cell body
A	0048306	molecular_function	calcium-dependent protein binding
A	0048741	biological_process	skeletal muscle fiber development
A	0051017	biological_process	actin filament bundle assembly
A	0090131	biological_process	mesenchyme migration
A	0098723	cellular_component	skeletal muscle myofibril
A	0140660	molecular_function	cytoskeletal motor activator activity
B	0000287	molecular_function	magnesium ion binding
B	0001725	cellular_component	stress fiber
B	0003785	molecular_function	actin monomer binding
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005523	molecular_function	tropomyosin binding
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0005865	cellular_component	striated muscle thin filament
B	0005884	cellular_component	actin filament
B	0010628	biological_process	positive regulation of gene expression
B	0016887	molecular_function	ATP hydrolysis activity
B	0019904	molecular_function	protein domain specific binding
B	0030027	cellular_component	lamellipodium
B	0030041	biological_process	actin filament polymerization
B	0030175	cellular_component	filopodium
B	0030240	biological_process	skeletal muscle thin filament assembly
B	0031013	molecular_function	troponin I binding
B	0031432	molecular_function	titin binding
B	0031941	cellular_component	filamentous actin
B	0032036	molecular_function	myosin heavy chain binding
B	0032432	cellular_component	actin filament bundle
B	0042802	molecular_function	identical protein binding
B	0044297	cellular_component	cell body
B	0048306	molecular_function	calcium-dependent protein binding
B	0048741	biological_process	skeletal muscle fiber development
B	0051017	biological_process	actin filament bundle assembly
B	0090131	biological_process	mesenchyme migration
B	0098723	cellular_component	skeletal muscle myofibril
B	0140660	molecular_function	cytoskeletal motor activator activity
C	0000287	molecular_function	magnesium ion binding
C	0001725	cellular_component	stress fiber
C	0003785	molecular_function	actin monomer binding
C	0005509	molecular_function	calcium ion binding
C	0005515	molecular_function	protein binding
C	0005523	molecular_function	tropomyosin binding
C	0005737	cellular_component	cytoplasm
C	0005856	cellular_component	cytoskeleton
C	0005865	cellular_component	striated muscle thin filament
C	0005884	cellular_component	actin filament
C	0010628	biological_process	positive regulation of gene expression
C	0016887	molecular_function	ATP hydrolysis activity
C	0019904	molecular_function	protein domain specific binding
C	0030027	cellular_component	lamellipodium
C	0030041	biological_process	actin filament polymerization
C	0030175	cellular_component	filopodium
C	0030240	biological_process	skeletal muscle thin filament assembly
C	0031013	molecular_function	troponin I binding
C	0031432	molecular_function	titin binding
C	0031941	cellular_component	filamentous actin
C	0032036	molecular_function	myosin heavy chain binding
C	0032432	cellular_component	actin filament bundle
C	0042802	molecular_function	identical protein binding
C	0044297	cellular_component	cell body
C	0048306	molecular_function	calcium-dependent protein binding
C	0048741	biological_process	skeletal muscle fiber development
C	0051017	biological_process	actin filament bundle assembly
C	0090131	biological_process	mesenchyme migration
C	0098723	cellular_component	skeletal muscle myofibril
C	0140660	molecular_function	cytoskeletal motor activator activity
D	0000287	molecular_function	magnesium ion binding
D	0001725	cellular_component	stress fiber
D	0003785	molecular_function	actin monomer binding
D	0005509	molecular_function	calcium ion binding
D	0005515	molecular_function	protein binding
D	0005523	molecular_function	tropomyosin binding
D	0005737	cellular_component	cytoplasm
D	0005856	cellular_component	cytoskeleton
D	0005865	cellular_component	striated muscle thin filament
D	0005884	cellular_component	actin filament
D	0010628	biological_process	positive regulation of gene expression
D	0016887	molecular_function	ATP hydrolysis activity
D	0019904	molecular_function	protein domain specific binding
D	0030027	cellular_component	lamellipodium
D	0030041	biological_process	actin filament polymerization
D	0030175	cellular_component	filopodium
D	0030240	biological_process	skeletal muscle thin filament assembly
D	0031013	molecular_function	troponin I binding
D	0031432	molecular_function	titin binding
D	0031941	cellular_component	filamentous actin
D	0032036	molecular_function	myosin heavy chain binding
D	0032432	cellular_component	actin filament bundle
D	0042802	molecular_function	identical protein binding
D	0044297	cellular_component	cell body
D	0048306	molecular_function	calcium-dependent protein binding
D	0048741	biological_process	skeletal muscle fiber development
D	0051017	biological_process	actin filament bundle assembly
D	0090131	biological_process	mesenchyme migration
D	0098723	cellular_component	skeletal muscle myofibril
D	0140660	molecular_function	cytoskeletal motor activator activity
Q	0007165	biological_process	signal transduction
R	0007165	biological_process	signal transduction
S	0007165	biological_process	signal transduction
T	0007165	biological_process	signal transduction

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue EDO B 401

Chain	Residue
B	TYR133
B	TYR143
B	LEU346
B	PHE375
R	ARG582

site_id	AC2
Number of Residues	12
Details	binding site for residue LAB B 402

Chain	Residue
B	TYR69
B	ASP157
B	ARG183
B	THR186
B	ARG206
B	GLU207
B	ARG210
B	HOH509
B	GLY15
B	LEU16
B	PRO32
B	GLN59

site_id	AC3
Number of Residues	22
Details	binding site for residue ATP B 403

Chain	Residue
B	GLY13
B	SER14
B	GLY15
B	LEU16
B	LYS18
B	GLY156
B	ASP157
B	GLY158
B	VAL159
B	ARG210
B	LYS213
B	GLU214
B	GLY302
B	THR303
B	MET305
B	TYR306
B	LYS336
B	MG404
B	HOH501
B	HOH515
B	HOH518
B	HOH522

site_id	AC4
Number of Residues	2
Details	binding site for residue MG B 404

Chain	Residue
B	ATP403
B	HOH522

site_id	AC5
Number of Residues	6
Details	binding site for residue EDO A 401

Chain	Residue
A	TYR133
A	ALA135
A	TYR143
A	PHE375
A	HOH504
S	ARG582

site_id	AC6
Number of Residues	11
Details	binding site for residue LAB A 402

Chain	Residue
A	GLY15
A	LEU16
A	PRO32
A	ILE34
A	TYR69
A	ASP157
A	ARG183
A	THR186
A	ARG206
A	GLU207
A	ARG210

site_id	AC7
Number of Residues	22
Details	binding site for residue ATP A 403

Chain	Residue
A	GLY13
A	SER14
A	GLY15
A	LEU16
A	LYS18
A	GLY156
A	ASP157
A	GLY158
A	VAL159
A	ARG210
A	LYS213
A	GLU214
A	GLY302
A	THR303
A	MET305
A	TYR306
A	LYS336
A	MG404
A	HOH511
A	HOH515
A	HOH520
A	HOH521

site_id	AC8
Number of Residues	5
Details	binding site for residue MG A 404

Chain	Residue
A	ATP403
A	HOH507
A	HOH515
A	HOH520
A	HOH521

site_id	AC9
Number of Residues	3
Details	binding site for residue EDO C 401

Chain	Residue
C	TYR133
C	TYR143
C	PHE375

site_id	AD1
Number of Residues	13
Details	binding site for residue LAB C 402

Chain	Residue
C	LYS213
C	ATP403
C	GLY15
C	LEU16
C	PRO32
C	TYR69
C	ASP157
C	GLY182
C	ARG183
C	THR186
C	ARG206
C	GLU207
C	ARG210

site_id	AD2
Number of Residues	22
Details	binding site for residue ATP C 403

Chain	Residue
C	GLY13
C	SER14
C	GLY15
C	LEU16
C	LYS18
C	GLY156
C	ASP157
C	GLY158
C	VAL159
C	ARG210
C	LYS213
C	GLU214
C	GLY301
C	GLY302
C	THR303
C	MET305
C	TYR306
C	LAB402
C	MG404
C	HOH508
C	HOH517
C	HOH523

site_id	AD3
Number of Residues	5
Details	binding site for residue MG C 404

Chain	Residue
C	ATP403
C	HOH503
C	HOH508
C	HOH517
C	HOH524

site_id	AD4
Number of Residues	4
Details	binding site for residue EDO D 401

Chain	Residue
D	TYR133
D	TYR143
D	PHE375
Q	ARG582

site_id	AD5
Number of Residues	11
Details	binding site for residue LAB D 402

Chain	Residue
D	GLY15
D	LEU16
D	PRO32
D	TYR69
D	ASP157
D	ARG183
D	THR186
D	ARG206
D	GLU207
D	ARG210
D	ATP403

site_id	AD6
Number of Residues	22
Details	binding site for residue ATP D 403

Chain	Residue
D	GLY13
D	SER14
D	GLY15
D	LEU16
D	LYS18
D	GLY156
D	ASP157
D	GLY158
D	VAL159
D	ARG210
D	LYS213
D	GLU214
D	GLY302
D	THR303
D	MET305
D	TYR306
D	LAB402
D	MG404
D	HOH502
D	HOH505
D	HOH509
D	HOH511

site_id	AD7
Number of Residues	4
Details	binding site for residue MG D 404

Chain	Residue
D	ATP403
D	HOH502
D	HOH505
D	HOH509

site_id	AD8
Number of Residues	5
Details	binding site for residue EDO R 801

Chain	Residue
B	ARG177
B	ASP179
R	LYS647
R	PHE650
R	ALA651

site_id	AD9
Number of Residues	8
Details	binding site for residue EDO Q 801

Chain	Residue
D	LEU110
D	PRO172
D	HIS173
D	ILE175
Q	GLN597
Q	PHE650
Q	ASN653
Q	HIS654

site_id	AE1
Number of Residues	5
Details	binding site for residue EDO S 801

Chain	Residue
S	VAL638
S	SER639
S	GLY640
S	GLY673
S	LYS676

site_id	AE2
Number of Residues	2
Details	binding site for residue EDO S 802

Chain	Residue
S	ASN690
S	ASP694

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	TYR53-GLY63

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

Chain	Residue	Details
B	TRP356-GLU364

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

Chain	Residue	Details
B	LEU104-ARG116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
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_FI2
Number of Residues	2
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
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_FI4
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_FI5
Number of Residues	4
Details	Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Site: {"description":"Arginine finger; crucial for GTP hydrolysis by stabilizing the transition state","evidences":[{"source":"PROSITE-ProRule","id":"PRU00172","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)