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6Z47

Smooth muscle myosin shutdown state heads region

Functional Information from GO Data
ChainGOidnamespacecontents
A0000146molecular_functionmicrofilament motor activity
A0000166molecular_functionnucleotide binding
A0003774molecular_functioncytoskeletal motor activity
A0003779molecular_functionactin binding
A0005516molecular_functioncalmodulin binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0016459cellular_componentmyosin complex
A0016460cellular_componentmyosin II complex
A0030016cellular_componentmyofibril
A0031032biological_processactomyosin structure organization
A0032982cellular_componentmyosin filament
A0043531molecular_functionADP binding
A0051015molecular_functionactin filament binding
A0097435biological_processsupramolecular fiber organization
A0099512cellular_componentsupramolecular fiber
B0000146molecular_functionmicrofilament motor activity
B0000166molecular_functionnucleotide binding
B0003774molecular_functioncytoskeletal motor activity
B0003779molecular_functionactin binding
B0005516molecular_functioncalmodulin binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0016459cellular_componentmyosin complex
B0016460cellular_componentmyosin II complex
B0030016cellular_componentmyofibril
B0031032biological_processactomyosin structure organization
B0032982cellular_componentmyosin filament
B0043531molecular_functionADP binding
B0051015molecular_functionactin filament binding
B0097435biological_processsupramolecular fiber organization
B0099512cellular_componentsupramolecular fiber
C0005509molecular_functioncalcium ion binding
C0005829cellular_componentcytosol
C0008307molecular_functionstructural constituent of muscle
C0016459cellular_componentmyosin complex
C0016460cellular_componentmyosin II complex
D0005509molecular_functioncalcium ion binding
D0005829cellular_componentcytosol
D0008307molecular_functionstructural constituent of muscle
D0016459cellular_componentmyosin complex
D0016460cellular_componentmyosin II complex
E0005509molecular_functioncalcium ion binding
E0046872molecular_functionmetal ion binding
F0005509molecular_functioncalcium ion binding
F0046872molecular_functionmetal ion binding
G0000146molecular_functionmicrofilament motor activity
G0000166molecular_functionnucleotide binding
G0003774molecular_functioncytoskeletal motor activity
G0003779molecular_functionactin binding
G0005516molecular_functioncalmodulin binding
G0005524molecular_functionATP binding
G0005737cellular_componentcytoplasm
G0016459cellular_componentmyosin complex
G0016460cellular_componentmyosin II complex
G0030016cellular_componentmyofibril
G0031032biological_processactomyosin structure organization
G0032982cellular_componentmyosin filament
G0043531molecular_functionADP binding
G0051015molecular_functionactin filament binding
G0097435biological_processsupramolecular fiber organization
G0099512cellular_componentsupramolecular fiber
H0000146molecular_functionmicrofilament motor activity
H0000166molecular_functionnucleotide binding
H0003774molecular_functioncytoskeletal motor activity
H0003779molecular_functionactin binding
H0005516molecular_functioncalmodulin binding
H0005524molecular_functionATP binding
H0005737cellular_componentcytoplasm
H0016459cellular_componentmyosin complex
H0016460cellular_componentmyosin II complex
H0030016cellular_componentmyofibril
H0031032biological_processactomyosin structure organization
H0032982cellular_componentmyosin filament
H0043531molecular_functionADP binding
H0051015molecular_functionactin filament binding
H0097435biological_processsupramolecular fiber organization
H0099512cellular_componentsupramolecular fiber
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MG A 2001
ChainResidue
ATHR184
ASER246
AADP2002
APO42003

site_idAC2
Number of Residues18
Detailsbinding site for residue ADP A 2002
ChainResidue
ATYR133
AGLU178
ASER179
AGLY180
AALA181
AGLY182
ALYS183
ATHR184
AGLU185
AASN242
AASN244
AMG2001
APO42003
AILE113
AASN125
APRO126
ATYR127
ALYS128

site_idAC3
Number of Residues9
Detailsbinding site for residue PO4 A 2003
ChainResidue
AGLU178
ASER179
ALYS183
AASN242
ASER245
ASER246
AGLY468
AMG2001
AADP2002

site_idAC4
Number of Residues5
Detailsbinding site for residue MG B 2001
ChainResidue
BTHR184
BASN244
BSER246
BADP2002
BPO42003

site_idAC5
Number of Residues14
Detailsbinding site for residue ADP B 2002
ChainResidue
BASN125
BPRO126
BLYS128
BTYR133
BSER179
BALA181
BGLY182
BLYS183
BTHR184
BGLU185
BASN242
BASN244
BMG2001
BPO42003

site_idAC6
Number of Residues9
Detailsbinding site for residue PO4 B 2003
ChainResidue
BSER179
BLYS183
BTHR184
BASN242
BASN244
BSER245
BSER246
BMG2001
BADP2002

site_idAC7
Number of Residues5
Detailsbinding site for residue MG E 201
ChainResidue
EASP42
EASN44
EASP46
EPHE48
EASP53

site_idAC8
Number of Residues5
Detailsbinding site for residue MG F 201
ChainResidue
FASP42
FASN44
FASP46
FPHE48
FASP53

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DQNRDGFIDkeDL
ChainResidueDetails
EASP42-LEU54

240971

PDB entries from 2025-08-27

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