Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9YR7

Cryo-EM structure of human beta-cardiac myosin bound to mavacamten in the interacting-heads motif and S2-FH undocked state

Functional Information from GO Data
ChainGOidnamespacecontents
A0006091biological_processgeneration of precursor metabolites and energy
A0008218biological_processbioluminescence
B0006091biological_processgeneration of precursor metabolites and energy
B0008218biological_processbioluminescence
C0000146molecular_functionmicrofilament motor activity
C0003774molecular_functioncytoskeletal motor activity
C0006936biological_processmuscle contraction
C0008307molecular_functionstructural constituent of muscle
C0016460cellular_componentmyosin II complex
C0016461cellular_componentunconventional myosin complex
C0030016cellular_componentmyofibril
C0030049biological_processmuscle filament sliding
C0043292cellular_componentcontractile muscle fiber
C0060048biological_processcardiac muscle contraction
D0000146molecular_functionmicrofilament motor activity
D0003774molecular_functioncytoskeletal motor activity
D0006936biological_processmuscle contraction
D0008307molecular_functionstructural constituent of muscle
D0016460cellular_componentmyosin II complex
D0016461cellular_componentunconventional myosin complex
D0030016cellular_componentmyofibril
D0030049biological_processmuscle filament sliding
D0043292cellular_componentcontractile muscle fiber
D0060048biological_processcardiac muscle contraction
E0005509molecular_functioncalcium ion binding
E0005737cellular_componentcytoplasm
E0006936biological_processmuscle contraction
E0007519biological_processskeletal muscle tissue development
E0008307molecular_functionstructural constituent of muscle
F0005509molecular_functioncalcium ion binding
F0005737cellular_componentcytoplasm
F0006936biological_processmuscle contraction
F0007519biological_processskeletal muscle tissue development
F0008307molecular_functionstructural constituent of muscle
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DQNRDGIIDkeDL
ChainResidueDetails
EASP38-LEU50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues98
DetailsDomain: {"description":"Myosin N-terminal SH3-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU01190","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues693
DetailsDomain: {"description":"Myosin motor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00782","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues58
DetailsDomain: {"description":"IQ","evidences":[{"source":"PROSITE-ProRule","id":"PRU00116","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues72
DetailsRegion: {"description":"Actin-binding"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues14
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P02563","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues140
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues140
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P02600","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P02600","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues6
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04466","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04466","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

254227

PDB entries from 2026-05-27

PDB statisticsPDBj update infoContact PDBjnumon