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3I5I

The crystal structure of squid myosin S1 in the presence of SO4 2-

Replaces:  2EKW
Functional Information from GO Data
ChainGOidnamespacecontents
A0003774molecular_functioncytoskeletal motor activity
A0005524molecular_functionATP binding
A0016459cellular_componentmyosin complex
A0051015molecular_functionactin filament binding
B0005509molecular_functioncalcium ion binding
B0005737cellular_componentcytoplasm
B0016459cellular_componentmyosin complex
B0016460cellular_componentmyosin II complex
B0032036molecular_functionmyosin heavy chain binding
B0046872molecular_functionmetal ion binding
C0005509molecular_functioncalcium ion binding
C0005859cellular_componentmuscle myosin complex
C0016459cellular_componentmyosin complex
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1001
ChainResidue
AGLU177
ASER178
AGLY179
AALA180
AGLY181
ALYS182
ATHR183

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 2001
ChainResidue
CGLY23
CARG24
CASP25
CASP27
CASP19
CASP22

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DQDRDGFIGmeDL
ChainResidueDetails
BASP26-LEU38

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
BASP26
BASP28
BASP30
BASP37

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Blocked amino end (Ala)
ChainResidueDetails
BALA1

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1vom
ChainResidueDetails
AGLY466
AGLY179
AASN242
AGLU468

226707

PDB entries from 2024-10-30

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