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3MYL

Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236

Functional Information from GO Data
ChainGOidnamespacecontents
X0003774molecular_functioncytoskeletal motor activity
X0005524molecular_functionATP binding
X0016459cellular_componentmyosin complex
X0051015molecular_functionactin filament binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG X 998
ChainResidue
XTHR186
XSER237
XPOP999
XHOH1111
XHOH1129

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE POP X 999
ChainResidue
XGLY184
XLYS185
XTHR186
XASN233
XALA236
XSER237
XMG998
XHOH1118
XHOH1129
XHOH1262
XHOH1301
XHOH1781
XGLU180
XSER181
XGLY182
XALA183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING:
ChainResidueDetails
XGLY179

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6,N6-dimethyllysine => ECO:0000255
ChainResidueDetails
XLYS130

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 534
ChainResidueDetails
XSER181proton acceptor, proton donor, proton relay
XGLY182electrostatic stabiliser
XTHR186metal ligand
XASN233electrostatic stabiliser
XALA236proton acceptor, proton donor, proton relay
XSER237metal ligand
XGLY457electrostatic stabiliser
XGLU459electrostatic stabiliser, proton acceptor, proton donor

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PDB entries from 2024-06-19

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