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5NUG

Motor domains from human cytoplasmic dynein-1 in the phi-particle conformation

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
A0005858cellular_componentaxonemal dynein complex
A0005868cellular_componentcytoplasmic dynein complex
A0005874cellular_componentmicrotubule
A0005881cellular_componentcytoplasmic microtubule
A0005938cellular_componentcell cortex
A0007018biological_processmicrotubule-based movement
A0007049biological_processcell cycle
A0007052biological_processmitotic spindle organization
A0007097biological_processnuclear migration
A0008090biological_processretrograde axonal transport
A0008569molecular_functionminus-end-directed microtubule motor activity
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
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
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
B0000166molecular_functionnucleotide binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005858cellular_componentaxonemal dynein complex
B0005868cellular_componentcytoplasmic dynein complex
B0005874cellular_componentmicrotubule
B0005881cellular_componentcytoplasmic microtubule
B0005938cellular_componentcell cortex
B0007018biological_processmicrotubule-based movement
B0007049biological_processcell cycle
B0007052biological_processmitotic spindle organization
B0007097biological_processnuclear migration
B0008090biological_processretrograde axonal transport
B0008569molecular_functionminus-end-directed microtubule motor activity
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0030175cellular_componentfilopodium
B0030286cellular_componentdynein complex
B0031122biological_processcytoplasmic microtubule organization
B0032388biological_processpositive regulation of intracellular transport
B0033962biological_processP-body assembly
B0034063biological_processstress granule assembly
B0035578cellular_componentazurophil granule lumen
B0045505molecular_functiondynein intermediate chain binding
B0051293biological_processestablishment of spindle localization
B0051301biological_processcell division
B0051959molecular_functiondynein light intermediate chain binding
B0060236biological_processregulation of mitotic spindle organization
B0070062cellular_componentextracellular exosome
B0090235biological_processregulation of metaphase plate congression
B0120162biological_processpositive regulation of cold-induced thermogenesis
B1904115cellular_componentaxon cytoplasm
B1905832biological_processpositive regulation of spindle assembly
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue ADP A 4801
ChainResidue
ALEU1879
AILE2049
ALEU2090
AARG2091
ALYS2094
AASP2320
AASP2321
AARG2358
AVAL1880
ATHR1885
AGLY1909
AGLY1911
ALYS1912
ATHR1913
AGLU1914
AASP1958

site_idAC2
Number of Residues18
Detailsbinding site for residue ATP A 4802
ChainResidue
ALEU2191
ATHR2192
ATRP2203
ASER2226
AGLY2227
ASER2228
AGLY2229
ALYS2230
ASER2231
AMET2232
AGLU2344
ALEU2369
AMET2373
AASN2377
AARG2684
AARG2726
AARG2729
AMG4803

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 4803
ChainResidue
ALYS2230
ASER2231
AGLU2344
AGLU2688
AATP4802

site_idAC4
Number of Residues14
Detailsbinding site for residue ADP A 4804
ChainResidue
ATHR2571
ATHR2574
APRO2597
AGLY2598
ASER2599
AGLY2600
ALYS2601
ATHR2602
AMET2603
APRO2739
AILE2747
APRO2796
AARG2797
ATHR2800

site_idAC5
Number of Residues13
Detailsbinding site for residue ADP A 4805
ChainResidue
AVAL2907
ALEU2909
AVAL2910
ASER2939
AGLY2940
AALA2941
AGLY2942
ALYS2943
ATHR2944
ATHR2945
ATRP3097
AARG3174
ALEU3177

site_idAC6
Number of Residues16
Detailsbinding site for residue ADP B 4801
ChainResidue
BLEU1879
BVAL1880
BTHR1885
BGLY1909
BGLY1911
BLYS1912
BTHR1913
BGLU1914
BASP1958
BILE2049
BLEU2090
BARG2091
BLYS2094
BASP2320
BASP2321
BARG2358

site_idAC7
Number of Residues18
Detailsbinding site for residue ATP B 4802
ChainResidue
BMG4803
BLEU2191
BTHR2192
BTRP2203
BSER2226
BGLY2227
BSER2228
BGLY2229
BLYS2230
BSER2231
BMET2232
BGLU2344
BLEU2369
BMET2373
BASN2377
BARG2684
BARG2726
BARG2729

site_idAC8
Number of Residues5
Detailsbinding site for residue MG B 4803
ChainResidue
BLYS2230
BSER2231
BGLU2344
BGLU2688
BATP4802

site_idAC9
Number of Residues14
Detailsbinding site for residue ADP B 4804
ChainResidue
BTHR2571
BTHR2574
BPRO2597
BGLY2598
BSER2599
BGLY2600
BLYS2601
BTHR2602
BMET2603
BPRO2739
BILE2747
BPRO2796
BARG2797
BTHR2800

site_idAD1
Number of Residues13
Detailsbinding site for residue ADP B 4805
ChainResidue
BVAL2907
BLEU2909
BVAL2910
BSER2939
BGLY2940
BALA2941
BGLY2942
BLYS2943
BTHR2944
BTHR2945
BTRP3097
BARG3174
BLEU3177

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 Residues8
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY1906
AGLY2224
AGLY2595
AGLY2937
BGLY1906
BGLY2224
BGLY2595
BGLY2937

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:22223895
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER70
ASER4162
BSER70
BSER4162

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS1125
ALYS3480
ALYS4283
BLYS1125
BLYS3480
BLYS4283

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9JHU4
ChainResidueDetails
ASER1230
BSER1230

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR4366
BTHR4366

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER4368
BSER4368

218853

PDB entries from 2024-04-24

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