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9BMS

State-2 of motor domain from full-length human dynein-1 in 5 mM ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005868cellular_componentcytoplasmic dynein complex
A0005874cellular_componentmicrotubule
A0005881cellular_componentcytoplasmic microtubule
A0005938cellular_componentcell cortex
A0007052biological_processmitotic spindle organization
A0007097biological_processnuclear migration
A0008090biological_processretrograde axonal transport
A0008569molecular_functionminus-end-directed microtubule motor activity
A0016020cellular_componentmembrane
A0030175cellular_componentfilopodium
A0030286cellular_componentdynein complex
A0031122biological_processcytoplasmic microtubule organization
A0032388biological_processpositive regulation of intracellular transport
A0033962biological_processP-body assembly
A0034063biological_processstress granule assembly
A0035578cellular_componentazurophil granule lumen
A0042802molecular_functionidentical protein binding
A0045505molecular_functiondynein intermediate chain binding
A0051293biological_processestablishment of spindle localization
A0051301biological_processcell division
A0051959molecular_functiondynein light intermediate chain binding
A0060236biological_processregulation of mitotic spindle organization
A0070062cellular_componentextracellular exosome
A0090235biological_processregulation of metaphase plate congression
A0120162biological_processpositive regulation of cold-induced thermogenesis
A1904115cellular_componentaxon cytoplasm
A1905832biological_processpositive regulation of spindle assembly
Functional Information from PROSITE/UniProt
site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. INHGLMMVGPS
ChainResidueDetails
AILE2216-SER2226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues231
DetailsRegion: {"description":"AAA 1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues249
DetailsRegion: {"description":"AAA 3","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues269
DetailsRegion: {"description":"AAA 4","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues229
DetailsRegion: {"description":"AAA 5","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues216
DetailsRegion: {"description":"AAA 6","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues63
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues28
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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