Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6RZA

Cryo-EM structure of the human inner arm dynein DNAH7 microtubule binding domain bound to microtubules

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0003924molecular_functionGTPase activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0007017biological_processmicrotubule-based process
A0015630cellular_componentmicrotubule cytoskeleton
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0003924molecular_functionGTPase activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000226biological_processmicrotubule cytoskeleton organization
C0000278biological_processmitotic cell cycle
C0003924molecular_functionGTPase activity
C0005200molecular_functionstructural constituent of cytoskeleton
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0007017biological_processmicrotubule-based process
C0015630cellular_componentmicrotubule cytoskeleton
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0000226biological_processmicrotubule cytoskeleton organization
D0000278biological_processmitotic cell cycle
D0003924molecular_functionGTPase activity
D0005200molecular_functionstructural constituent of cytoskeleton
D0005515molecular_functionprotein binding
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005874cellular_componentmicrotubule
D0007017biological_processmicrotubule-based process
D0046872molecular_functionmetal ion binding
X0007018biological_processmicrotubule-based movement
X0008569molecular_functionminus-end-directed microtubule motor activity
X0030286cellular_componentdynein complex
X0045505molecular_functiondynein intermediate chain binding
X0051959molecular_functiondynein light intermediate chain binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
AASN101
ASER140
AGLY143
AGLY144
ATHR145
AGLY146
AILE171
ATHR179
AASN206
ATYR224
AGLN11
ALEU227
AASN228
AMG502
BLYS252
AALA12
AGLN15
AASP69
AGLU71
AASP98
AALA99
AALA100

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 502
ChainResidue
AGLN11
AGLU71
AGTP501

site_idAC3
Number of Residues13
Detailsbinding site for residue GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BASN99
BGLY141
BGLY142
BTHR143
BASP177
BGLU181
BASN204
BTYR222
BASN226

site_idAC4
Number of Residues12
Detailsbinding site for residue TA1 B 502
ChainResidue
BGLU22
BASP26
BASP224
BHIS227
BLEU228
BALA231
BPRO272
BTHR274
BARG318
BPRO358
BARG359
BLEU361

site_idAC5
Number of Residues23
Detailsbinding site for residue GTP C 501
ChainResidue
CGLY10
CGLN11
CALA12
CGLN15
CASP69
CGLU71
CASP98
CALA99
CALA100
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CILE171
CTHR179
CASN206
CTYR224
CLEU227
CASN228
CMG502
DLYS252

site_idAC6
Number of Residues3
Detailsbinding site for residue MG C 502
ChainResidue
CGLN11
CGLU71
CGTP501

site_idAC7
Number of Residues13
Detailsbinding site for residue GDP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DASN99
DGLY141
DGLY142
DTHR143
DASP177
DGLU181
DASN204
DTYR222
DASN226

site_idAC8
Number of Residues13
Detailsbinding site for residue TA1 D 502
ChainResidue
DARG318
DPRO358
DARG359
DLEU361
DGLU22
DASP26
DASP224
DHIS227
DLEU228
DALA231
DPRO272
DTHR274
DGLN279

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
BGLY140-GLY146
AGLY142-GLY148

site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
BMET1-ILE4

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q13509
ChainResidueDetails
BGLN11
DGLY142
DTHR143
DGLY144
DASN204
DASN226
BSER138
BGLY142
BTHR143
BGLY144
BASN204
BASN226
DGLN11
DSER138

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
BGLU69
CGLU71
CSER140
CGLY144
CTHR145
CTHR179
CASN206
CASN228
DGLU69
ASER140
AGLY144
ATHR145
ATHR179
AASN206
AASN228
CGLN11

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BSER40
DSER40

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BLYS58
DLYS58
CSER48
CSER232

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885
ChainResidueDetails
BSER172
DSER172

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BTHR285
BTHR290
DTHR285
DTHR290

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BARG318
DARG318
ALYS370
CLYS326
CLYS370

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS58
DLYS58

site_idSWS_FT_FI9
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS324
DLYS324

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon