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2BKH

Myosin VI nucleotide-free (MDInsert2) crystal structure

Functional Information from GO Data
ChainGOidnamespacecontents
A0003774molecular_functioncytoskeletal motor activity
A0005524molecular_functionATP binding
A0016459cellular_componentmyosin complex
A0051015molecular_functionactin filament binding
B0000226biological_processmicrotubule cytoskeleton organization
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005814cellular_componentcentriole
B0005819cellular_componentspindle
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005938cellular_componentcell cortex
B0007099biological_processcentriole replication
B0007605biological_processsensory perception of sound
B0007608biological_processsensory perception of smell
B0016028cellular_componentrhabdomere
B0016056biological_processG protein-coupled opsin signaling pathway
B0016059biological_processnegative regulation of opsin-mediated signaling pathway
B0016060biological_processnegative regulation of phospholipase C-activating phototransduction signaling pathway
B0016247molecular_functionchannel regulator activity
B0030048biological_processactin filament-based movement
B0030234molecular_functionenzyme regulator activity
B0030496cellular_componentmidbody
B0031475cellular_componentmyosin V complex
B0031476cellular_componentmyosin VI complex
B0031477cellular_componentmyosin VII complex
B0031489molecular_functionmyosin V binding
B0032036molecular_functionmyosin heavy chain binding
B0042052biological_processrhabdomere development
B0046716biological_processmuscle cell cellular homeostasis
B0046872molecular_functionmetal ion binding
B0048102biological_processautophagic cell death
B0050911biological_processdetection of chemical stimulus involved in sensory perception of smell
B0051383biological_processkinetochore organization
B0070855molecular_functionmyosin VI head/neck binding
B0071361biological_processcellular response to ethanol
B0072499biological_processphotoreceptor cell axon guidance
B0072686cellular_componentmitotic spindle
B0097431cellular_componentmitotic spindle pole
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B1148
ChainResidue
BASP20
BASP22
BASP24
BTHR26
BGLU31

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B1149
ChainResidue
BGLU67
BASP56
BASP58
BASN60
BTHR62

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B1150
ChainResidue
BASP93
BASP95
BASN97
BPHE99
BGLU104

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B1151
ChainResidue
BASP129
BASP131
BASP133
BGLN135
BGLU140

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A1813
ChainResidue
ASER150
AASN477
AGLN481
APHE484
APHE582
AARG667
ASER692
AHOH2278

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A1814
ChainResidue
AALA253
AALA255
AGLN290
AILE291
ALEU292
AHIS314

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A1815
ChainResidue
AGLU231
ALYS232
ASER233
ACYS472

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A1816
ChainResidue
AARG205
APHE206
AGLY207
ALEU229
AGLU231
APHE647
AHOH2103

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A1817
ChainResidue
AARG199
AGLU461
ATYR462
ASER687
AHOH2155

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A1818
ChainResidue
AHIS264
AHIS346
AASN349
AGLN370
AALA371

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
BASP20-LEU32
BASP56-PHE68
BASP93-LEU105
BASP129-PHE141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsRegion: {"description":"Responsible for slow ATPase activity","evidences":[{"source":"PubMed","id":"15944696","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsRegion: {"description":"Actin-binding","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsRegion: {"description":"Required for binding calmodulin","evidences":[{"source":"PubMed","id":"15037754","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9UM54","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"12682054","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q64331","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues35
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues19
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsSite: {"description":"Not N6-methylated"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"17610210","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1vom
ChainResidueDetails
AGLY459
AGLU461
AASN200
AGLY154

243083

PDB entries from 2025-10-15

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