2V51

Structure of MAL-RPEL1 complexed to actin

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0000166	molecular_function	nucleotide binding
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	0005524	molecular_function	ATP 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	0016787	molecular_function	hydrolase 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
D	0000166	molecular_function	nucleotide binding
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	0005524	molecular_function	ATP 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	0016787	molecular_function	hydrolase 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ATP B1372

Chain	Residue
B	GLY13
B	GLY182
B	ARG210
B	LYS213
B	GLU214
B	GLY301
B	GLY302
B	MET305
B	TYR306
B	LYS336
B	CA1373
B	SER14
B	LAB1374
B	HOH2038
B	HOH2076
B	HOH2093
B	HOH2101
B	HOH2102
B	HOH2103
B	GLY15
B	LEU16
B	LYS18
B	GLY156
B	ASP157
B	GLY158
B	VAL159

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B1373

Chain	Residue
B	ATP1372
B	HOH2002
B	HOH2003
B	HOH2038
B	HOH2102

---

site_id	AC3
Number of Residues	27
Details	BINDING SITE FOR RESIDUE ATP D1372

Chain	Residue
D	GLY13
D	SER14
D	GLY15
D	LEU16
D	LYS18
D	GLY156
D	ASP157
D	GLY158
D	VAL159
D	GLY182
D	ARG210
D	LYS213
D	GLU214
D	GLY301
D	GLY302
D	MET305
D	TYR306
D	LYS336
D	CA1373
D	LAB1374
D	HOH2042
D	HOH2043
D	HOH2049
D	HOH2080
D	HOH2093
D	HOH2095
D	HOH2096

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D1373

Chain	Residue
D	ATP1372
D	HOH2003
D	HOH2004
D	HOH2042
D	HOH2049

---

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE LAB B1374

Chain	Residue
B	GLY15
B	PRO32
B	TYR69
B	ASP157
B	THR186
B	ARG206
B	GLU207
B	ARG210
B	LYS213
B	ATP1372

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG B1375

Chain	Residue
B	LYS238
B	ARG254

---

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE LAB D1374

Chain	Residue
D	GLY15
D	ILE34
D	TYR69
D	ASP157
D	ARG183
D	THR186
D	ARG206
D	GLU207
D	ARG210
D	LYS213
D	ATP1372
D	HOH2097

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SCN B1376

Chain	Residue
B	GLY197
B	SER199

---

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SCN D1375

Chain	Residue
D	GLY197
D	SER199

---

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SCN B1377

Chain	Residue
B	TRP79

---

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	50
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":"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_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	50
Details	Repeat: {"description":"RPEL 1"}

Chain

Residue

Details

---