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2MYS

MYOSIN SUBFRAGMENT-1, ALPHA CARBON COORDINATES ONLY FOR THE TWO LIGHT CHAINS

Replaces:  1MYS
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
B0006936biological_processmuscle contraction
B0007519biological_processskeletal muscle tissue development
B0016459cellular_componentmyosin complex
B0046872molecular_functionmetal ion binding
C0005509molecular_functioncalcium ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 5000
ChainResidue
ASER181
AGLY182
AALA183
AGLY184
ALYS185
ATHR186
AASN240
ASER243

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DQNADGIIDkdDL
ChainResidueDetails
BASP35-LEU47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Blocked amino end (Ser)
ChainResidueDetails
CPHE2
BASP39
BILE41
BARG48

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N,N,N-trimethylalanine => ECO:0000305|PubMed:3979397
ChainResidueDetails
BLYS2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000255
ChainResidueDetails
BVAL15

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:3467365
ChainResidueDetails
ATRP131
AASN552

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Pros-methylhistidine => ECO:0000269|PubMed:3467365
ChainResidueDetails
ATHR756

218853

PDB entries from 2024-04-24

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