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1QVI

Crystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Angstrom resolution: flexibility and function in the head

Functional Information from GO Data
ChainGOidnamespacecontents
A0003774molecular_functioncytoskeletal motor activity
A0005524molecular_functionATP binding
A0016459cellular_componentmyosin complex
A0051015molecular_functionactin filament binding
Y0005509molecular_functioncalcium ion binding
Y0016459cellular_componentmyosin complex
Y0046872molecular_functionmetal ion binding
Z0005509molecular_functioncalcium ion binding
Z0005859cellular_componentmuscle myosin complex
Z0016459cellular_componentmyosin complex
Z0016460cellular_componentmyosin II complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1997
ChainResidue
ATHR183
ASER241
AASP460
AVO41998
AADP1999

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE VO4 A 1998
ChainResidue
ASER240
ASER241
AGLY463
AMG1997
AADP1999
AHOH2020
ASER178
AGLY179
ALYS182
AASN237

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA Z 503
ChainResidue
ZASP19
ZASP22
ZGLY23
ZASP25
ZALA27

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG Y 502
ChainResidue
YASP28
YASP30
YASP32
YPHE34
YSER36
YASP39

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP A 1999
ChainResidue
AASN124
APRO125
ATYR126
AARG127
AARG128
ATYR132
AGLY179
AALA180
AGLY181
ALYS182
ATHR183
AGLU184
AASN237
AMG1997
AVO41998
AHOH2030

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DVDRDGFVSkeDI
ChainResidueDetails
YASP28-ILE40

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues50
DetailsDomain: {"description":"Myosin N-terminal SH3-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU01190","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues27
DetailsDomain: {"description":"IQ","evidences":[{"source":"PROSITE-ProRule","id":"PRU00116","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues22
DetailsRegion: {"description":"Actin-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00782","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues72
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues70
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1vom
ChainResidueDetails
AGLY179
AGLU465
AGLY463
AASN237

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PDB entries from 2025-10-22

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