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1JX2

CRYSTAL STRUCTURE OF THE NUCLEOTIDE-FREE DYNAMIN A GTPASE DOMAIN, DETERMINED AS MYOSIN FUSION

Functional Information from GO Data
ChainGOidnamespacecontents
A0003774molecular_functioncytoskeletal motor activity
A0003924molecular_functionGTPase activity
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0016459cellular_componentmyosin complex
A0051015molecular_functionactin filament binding
Functional Information from PROSITE/UniProt
site_idPS00410
Number of Residues10
DetailsG_DYNAMIN_1 Dynamin-type guanine nucleotide-binding (G) domain signature. LPRGSGIVTR
ChainResidueDetails
ALEU835-ARG844

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 Residues36
DetailsRegion: {"description":"Actin-binding"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6,N6-dimethyllysine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues7
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues17
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O00429","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1vom
ChainResidueDetails
AGLY193
AGLY468
AGLU470
AASN244

site_idMCSA1
Number of Residues8
DetailsM-CSA 534
ChainResidueDetails
ASER192proton acceptor, proton donor, proton relay
AGLY193electrostatic stabiliser
ATHR197metal ligand
AASN244electrostatic stabiliser
ASER247proton acceptor, proton donor, proton relay
ASER248metal ligand
AGLY468electrostatic stabiliser
AGLU470electrostatic stabiliser, proton acceptor, proton donor

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PDB entries from 2025-12-24

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