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3MYH

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 Residues6
DetailsBINDING SITE FOR RESIDUE MG X 997
ChainResidue
XTHR186
XSER237
XHOH780
XHOH787
XVO4998
XADP999

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE VO4 X 998
ChainResidue
XASN233
XALA236
XSER237
XGLY457
XHOH780
XHOH787
XHOH792
XMG997
XADP999
XSER181
XGLY182
XLYS185

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ADP X 999
ChainResidue
XASN127
XPRO128
XPHE129
XLYS130
XTYR135
XGLY182
XALA183
XGLY184
XLYS185
XTHR186
XGLU187
XASN233
XHOH774
XHOH777
XHOH780
XHOH787
XHOH908
XMG997
XVO4998
XHOH1016
XHOH1049

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE BIT X 800
ChainResidue
XARG238
XPHE239
XGLY240
XTYR261
XLEU262
XSER456
XGLU467
XCYS470
XTYR634
XLEU641
XHOH927

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 2024-07-24

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