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6FSA

Beta-Cardiac myosin post-rigor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000146molecular_functionmicrofilament motor activity
A0000166molecular_functionnucleotide binding
A0003774molecular_functioncytoskeletal motor activity
A0003779molecular_functionactin binding
A0005516molecular_functioncalmodulin binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0007512biological_processadult heart development
A0016459cellular_componentmyosin complex
A0016460cellular_componentmyosin II complex
A0030016cellular_componentmyofibril
A0030017cellular_componentsarcomere
A0030049biological_processmuscle filament sliding
A0032982cellular_componentmyosin filament
A0051015molecular_functionactin filament binding
A0060048biological_processcardiac muscle contraction
B0000146molecular_functionmicrofilament motor activity
B0000166molecular_functionnucleotide binding
B0003774molecular_functioncytoskeletal motor activity
B0003779molecular_functionactin binding
B0005516molecular_functioncalmodulin binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0007512biological_processadult heart development
B0016459cellular_componentmyosin complex
B0016460cellular_componentmyosin II complex
B0030016cellular_componentmyofibril
B0030017cellular_componentsarcomere
B0030049biological_processmuscle filament sliding
B0032982cellular_componentmyosin filament
B0051015molecular_functionactin filament binding
B0060048biological_processcardiac muscle contraction
D0005509molecular_functioncalcium ion binding
D0016459cellular_componentmyosin complex
D0016460cellular_componentmyosin II complex
H0005509molecular_functioncalcium ion binding
H0016459cellular_componentmyosin complex
H0016460cellular_componentmyosin II complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MG A 2001
ChainResidue
ATHR185
AASN240
ASER242
AADP2002

site_idAC2
Number of Residues25
Detailsbinding site for residue ADP A 2002
ChainResidue
ATYR134
AGLU179
ASER180
AGLY181
AALA182
AGLY183
ALYS184
ATHR185
AVAL186
AASN238
AMG2001
AHOH2144
AHOH2163
AHOH2167
AHOH2187
AHOH2226
AHOH2233
AHOH2276
AHOH2278
AHOH2330
AASN126
APRO127
ATYR128
AMLY129
ATRP130

site_idAC3
Number of Residues3
Detailsbinding site for residue FMT A 2003
ChainResidue
AHIS251
AARG453
ATYR455

site_idAC4
Number of Residues4
Detailsbinding site for residue FMT A 2004
ChainResidue
ASER271
AARG272
APHE275
AHOH2105

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 2005
ChainResidue
AGLY701
AHOH2109
AHOH2300
AHOH2464

site_idAC6
Number of Residues3
Detailsbinding site for residue MG B 2001
ChainResidue
BTHR185
BSER242
BADP2002

site_idAC7
Number of Residues19
Detailsbinding site for residue ADP B 2002
ChainResidue
BASN126
BPRO127
BMLY129
BTRP130
BTYR134
BGLU179
BSER180
BGLY181
BALA182
BGLY183
BLYS184
BTHR185
BVAL186
BASN238
BMG2001
BHOH2101
BHOH2185
BHOH2238
BHOH2250

site_idAC8
Number of Residues4
Detailsbinding site for residue FMT B 2003
ChainResidue
BGLY202
BGLU217
BLEU258
BHOH2171

site_idAC9
Number of Residues7
Detailsbinding site for residue FMT B 2004
ChainResidue
BGLU88
BTYR117
BARG147
BALA150
BPRO151
BPRO152
BHOH2256

site_idAD1
Number of Residues4
Detailsbinding site for residue FMT B 2005
ChainResidue
BTYR266
BLEU267
BTHR481
BHIS651

site_idAD2
Number of Residues7
Detailsbinding site for residue EDO B 2006
ChainResidue
BMET493
BGLY701
BILE702
BCYS705
BHOH2116
BHOH2122
BHOH2148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N,N,N-trimethylalanine => ECO:0000269|PubMed:3979397
ChainResidueDetails
DALA2
HALA2

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P16409
ChainResidueDetails
DTHR92
DTHR133
HTHR92
HTHR133

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P09542
ChainResidueDetails
DTHR131
HTHR131
ATHR1309
ATHR1513
BTHR378
BTHR1282
BTHR1309
BTHR1513

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P16409
ChainResidueDetails
DTYR134
HTYR134

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09542
ChainResidueDetails
DSER183
HSER183

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P02563
ChainResidueDetails
ATYR1308
BTYR1308

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02564
ChainResidueDetails
ASER1510
BSER1510

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PDB entries from 2025-07-02

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