6BIH

The Structure of the Actin-Smooth Muscle Myosin Motor Domain Complex in the Rigor State

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0000166	molecular_function	nucleotide binding
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	0005524	molecular_function	ATP 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	0016787	molecular_function	hydrolase 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
H	0003774	molecular_function	cytoskeletal motor activity
H	0005524	molecular_function	ATP binding
H	0016459	cellular_component	myosin complex
H	0051015	molecular_function	actin filament binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue ADP C 401

Chain	Residue
C	GLY15
C	TYR306
C	LYS336
C	LEU16
C	LYS18
C	ASP157
C	GLY158
C	GLU214
C	LYS215
C	GLY302
C	MET305

---

site_id	AC2
Number of Residues	5
Details	binding site for residue MG C 402

Chain	Residue
C	ASP154
C	SER300
C	GLY301
C	SER338
C	VAL339

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	TYR53-GLY63

---

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

Chain	Residue	Details
C	TRP356-GLU364

---

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

Chain	Residue	Details
C	LEU104-ARG116

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	22
Details	Region: {"description":"Actin-binding"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	7
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Blocked amino end (Ser)","evidences":[{"source":"PubMed","id":"3312184","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"3312184","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	25
Details	Region: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N-acetylaspartate; in Actin, alpha skeletal muscle","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
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_FI10
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---