Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4RWT

Structure of actin-Lmod complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000281	biological_process	mitotic cytokinesis
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005856	cellular_component	cytoskeleton
A	0006338	biological_process	chromatin remodeling
A	0007010	biological_process	cytoskeleton organization
A	0007291	biological_process	sperm individualization
A	0015629	cellular_component	actin cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0030723	biological_process	ovarian fusome organization
A	0031011	cellular_component	Ino80 complex
A	0032507	biological_process	maintenance of protein location in cell
A	0035060	cellular_component	brahma complex
A	0035148	biological_process	tube formation
A	0048468	biological_process	cell development
A	0048646	biological_process	anatomical structure formation involved in morphogenesis
B	0000166	molecular_function	nucleotide binding
B	0000281	biological_process	mitotic cytokinesis
B	0005200	molecular_function	structural constituent of cytoskeleton
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005856	cellular_component	cytoskeleton
B	0006338	biological_process	chromatin remodeling
B	0007010	biological_process	cytoskeleton organization
B	0007291	biological_process	sperm individualization
B	0015629	cellular_component	actin cytoskeleton
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0030723	biological_process	ovarian fusome organization
B	0031011	cellular_component	Ino80 complex
B	0032507	biological_process	maintenance of protein location in cell
B	0035060	cellular_component	brahma complex
B	0035148	biological_process	tube formation
B	0048468	biological_process	cell development
B	0048646	biological_process	anatomical structure formation involved in morphogenesis
C	0003779	molecular_function	actin binding
C	0003785	molecular_function	actin monomer binding
C	0005523	molecular_function	tropomyosin binding
C	0005856	cellular_component	cytoskeleton
C	0005865	cellular_component	striated muscle thin filament
C	0005884	cellular_component	actin filament
C	0006936	biological_process	muscle contraction
C	0007015	biological_process	actin filament organization
C	0030016	cellular_component	myofibril
C	0030017	cellular_component	sarcomere
C	0030041	biological_process	actin filament polymerization
C	0030239	biological_process	myofibril assembly
C	0030838	biological_process	positive regulation of actin filament polymerization
C	0031430	cellular_component	M band
C	0045010	biological_process	actin nucleation
C	0045214	biological_process	sarcomere organization
C	0051694	biological_process	pointed-end actin filament capping
D	0003779	molecular_function	actin binding
D	0003785	molecular_function	actin monomer binding
D	0005523	molecular_function	tropomyosin binding
D	0005856	cellular_component	cytoskeleton
D	0005865	cellular_component	striated muscle thin filament
D	0005884	cellular_component	actin filament
D	0006936	biological_process	muscle contraction
D	0007015	biological_process	actin filament organization
D	0030016	cellular_component	myofibril
D	0030017	cellular_component	sarcomere
D	0030041	biological_process	actin filament polymerization
D	0030239	biological_process	myofibril assembly
D	0030838	biological_process	positive regulation of actin filament polymerization
D	0031430	cellular_component	M band
D	0045010	biological_process	actin nucleation
D	0045214	biological_process	sarcomere organization
D	0051694	biological_process	pointed-end actin filament capping

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ANP A 401

Chain	Residue
A	GLY13
A	LYS213
A	GLU214
A	GLY302
A	MET305
A	TYR306
A	LYS336
A	MG402
A	SER14
A	GLY15
A	MET16
A	LYS18
A	GLY156
A	ASP157
A	GLY182
A	ARG210

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 402

Chain	Residue
A	GLN137
A	ANP401

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ANP B 401

Chain	Residue
B	GLY13
B	SER14
B	GLY15
B	MET16
B	LYS18
B	GLY156
B	ASP157
B	GLY182
B	ARG210
B	LYS213
B	GLU214
B	GLY302
B	THR303
B	MET305
B	TYR306
B	MG402

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 402

Chain	Residue
B	GLN137
B	ANP401

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	TYR53-GLY63

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

Chain	Residue	Details
A	TRP356-GLU364

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

Chain	Residue	Details
A	LEU104-ARG116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Modified residue: {"description":"Methionine sulfoxide","evidences":[{"source":"PubMed","id":"22116028","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"UniProtKB","id":"P02572","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	19
Details	Domain: {"description":"WH2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00406","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	19
Details	Region: {"description":"Interaction with actin 3","evidences":[{"source":"PubMed","id":"26417072","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	33
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	10
Details	Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	10
Details	Compositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

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