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2AKA

Structure of the nucleotide-free myosin II motor domain from Dictyostelium discoideum fused to the GTPase domain of dynamin 1 from Rattus norvegicus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003774molecular_functioncytoskeletal motor activity
A0005524molecular_functionATP binding
A0016459cellular_componentmyosin complex
A0051015molecular_functionactin filament binding
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
Functional Information from PROSITE/UniProt
site_idPS00410
Number of Residues10
DetailsG_DYNAMIN_1 Dynamin-type guanine nucleotide-binding (G) domain signature. LPRGSGIVTR
ChainResidueDetails
BLEU57-ARG66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues52
DetailsDomain: {"description":"Myosin N-terminal SH3-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU01190","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues673
DetailsDomain: {"description":"Myosin motor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00782","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues36
DetailsRegion: {"description":"Actin-binding"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6,N6-dimethyllysine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues266
DetailsDomain: {"description":"Dynamin-type G","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues7
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsRegion: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues3
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues13
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q05193","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P39053","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; alternate","evidences":[{"source":"UniProtKB","id":"P39053","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1vom
ChainResidueDetails
AGLU459
AGLY182
AGLY457
AASN233

site_idMCSA1
Number of Residues8
DetailsM-CSA 534
ChainResidueDetails
ASER181proton acceptor, proton donor, proton relay
AGLY182electrostatic stabiliser
ATHR186metal ligand
AASN233electrostatic stabiliser
ASER236proton acceptor, proton donor, proton relay
ASER237metal ligand
AGLY457electrostatic stabiliser
AGLU459electrostatic stabiliser, proton acceptor, proton donor

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PDB entries from 2025-12-24

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