1I84

CRYO-EM STRUCTURE OF THE HEAVY MEROMYOSIN SUBFRAGMENT OF CHICKEN GIZZARD SMOOTH MUSCLE MYOSIN WITH REGULATORY LIGHT CHAIN IN THE DEPHOSPHORYLATED STATE. ONLY C ALPHAS PROVIDED FOR REGULATORY LIGHT CHAIN. ONLY BACKBONE ATOMS PROVIDED FOR S2 FRAGMENT.

Functional Information from GO Data

Chain	GOid	namespace	contents
S	0003774	molecular_function	cytoskeletal motor activity
S	0005524	molecular_function	ATP binding
S	0016459	cellular_component	myosin complex
S	0051015	molecular_function	actin filament binding
T	0000146	molecular_function	microfilament motor activity
T	0000287	molecular_function	magnesium ion binding
T	0005509	molecular_function	calcium ion binding
T	0005515	molecular_function	protein binding
T	0005829	cellular_component	cytosol
T	0005859	cellular_component	muscle myosin complex
T	0008307	molecular_function	structural constituent of muscle
T	0016459	cellular_component	myosin complex
T	0016460	cellular_component	myosin II complex
T	0030239	biological_process	myofibril assembly
T	0031032	biological_process	actomyosin structure organization
T	0032036	molecular_function	myosin heavy chain binding
T	0042641	cellular_component	actomyosin
T	0043531	molecular_function	ADP binding
T	0045159	molecular_function	myosin II binding
T	0051015	molecular_function	actin filament binding
T	0097513	cellular_component	myosin II filament
U	0005509	molecular_function	calcium ion binding
U	0005737	cellular_component	cytoplasm
U	0006936	biological_process	muscle contraction
U	0007519	biological_process	skeletal muscle tissue development
U	0016459	cellular_component	myosin complex
U	0046872	molecular_function	metal ion binding
V	0003774	molecular_function	cytoskeletal motor activity
V	0005524	molecular_function	ATP binding
V	0016459	cellular_component	myosin complex
V	0051015	molecular_function	actin filament binding
W	0000146	molecular_function	microfilament motor activity
W	0000287	molecular_function	magnesium ion binding
W	0005509	molecular_function	calcium ion binding
W	0005515	molecular_function	protein binding
W	0005829	cellular_component	cytosol
W	0005859	cellular_component	muscle myosin complex
W	0008307	molecular_function	structural constituent of muscle
W	0016459	cellular_component	myosin complex
W	0016460	cellular_component	myosin II complex
W	0030239	biological_process	myofibril assembly
W	0031032	biological_process	actomyosin structure organization
W	0032036	molecular_function	myosin heavy chain binding
W	0042641	cellular_component	actomyosin
W	0043531	molecular_function	ADP binding
W	0045159	molecular_function	myosin II binding
W	0051015	molecular_function	actin filament binding
W	0097513	cellular_component	myosin II filament
Z	0005509	molecular_function	calcium ion binding
Z	0005737	cellular_component	cytoplasm
Z	0006936	biological_process	muscle contraction
Z	0007519	biological_process	skeletal muscle tissue development
Z	0016459	cellular_component	myosin complex
Z	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DQNADGIIDkdDL

Chain	Residue	Details
U	ASP35-LEU47

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	100
Details	Domain: {"description":"Myosin N-terminal SH3-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU01190","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	58
Details	Domain: {"description":"IQ","evidences":[{"source":"PROSITE-ProRule","id":"PRU00116","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	72
Details	Region: {"description":"Actin-binding"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	14
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Blocked amino end (Ser)","evidences":[{"source":"PubMed","id":"3312184","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"3312184","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	140
Details	Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	70
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	64
Details	Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1vom

Chain	Residue	Details
S	ASN242
S	GLY180
S	GLY468
S	GLU470

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1vom

Chain	Residue	Details
V	ASN242
V	GLY180
V	GLY468
V	GLU470

---