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5SZJ

Structure of human Rab10 in complex with the bMERB domain of Mical-cL

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000145cellular_componentexocyst
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005768cellular_componentendosome
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005912cellular_componentadherens junction
A0005925cellular_componentfocal adhesion
A0005929cellular_componentcilium
A0006887biological_processexocytosis
A0006893biological_processGolgi to plasma membrane transport
A0007409biological_processaxonogenesis
A0009306biological_processprotein secretion
A0010008cellular_componentendosome membrane
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0016192biological_processvesicle-mediated transport
A0016197biological_processendosomal transport
A0016787molecular_functionhydrolase activity
A0019003molecular_functionGDP binding
A0019882biological_processantigen processing and presentation
A0030659cellular_componentcytoplasmic vesicle membrane
A0030667cellular_componentsecretory granule membrane
A0030670cellular_componentphagocytic vesicle membrane
A0030859biological_processpolarized epithelial cell differentiation
A0031410cellular_componentcytoplasmic vesicle
A0031489molecular_functionmyosin V binding
A0032593cellular_componentinsulin-responsive compartment
A0032869biological_processcellular response to insulin stimulus
A0042995cellular_componentcell projection
A0043001biological_processGolgi to plasma membrane protein transport
A0045055biological_processregulated exocytosis
A0045200biological_processestablishment of neuroblast polarity
A0048471cellular_componentperinuclear region of cytoplasm
A0051668biological_processlocalization within membrane
A0055037cellular_componentrecycling endosome
A0055038cellular_componentrecycling endosome membrane
A0070062cellular_componentextracellular exosome
A0070382cellular_componentexocytic vesicle
A0071782cellular_componentendoplasmic reticulum tubular network
A0071786biological_processendoplasmic reticulum tubular network organization
A0072659biological_processprotein localization to plasma membrane
A0090150biological_processestablishment of protein localization to membrane
A0097051biological_processestablishment of protein localization to endoplasmic reticulum membrane
A0098609biological_processcell-cell adhesion
A0098641molecular_functioncadherin binding involved in cell-cell adhesion
A0099503cellular_componentsecretory vesicle
A0120025cellular_componentplasma membrane bounded cell projection
A1903361biological_processprotein localization to basolateral plasma membrane
Functional Information from PDB Data
site_idAC1
Number of Residues28
Detailsbinding site for residue GNP A 301
ChainResidue
ASER18
ATHR36
APHE38
ASER40
ATHR41
ATHR65
AALA66
AGLY67
AASN122
ALYS123
AASP125
AGLY19
AMET126
ASER152
AALA153
ALYS154
AMG302
AHOH405
AHOH409
AHOH412
AHOH414
AVAL20
AGLY21
ALYS22
ATHR23
ACYS24
APHE34
AASN35

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 302
ChainResidue
ATHR23
ATHR41
AASP64
AGNP301
AHOH405
AHOH414

site_idAC3
Number of Residues6
Detailsbinding site for residue PEG B 701
ChainResidue
ALYS47
BGLU617
BGLN620
BSER621
BGLU624
BARG660

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. LLLiGDSGVGKtcV
ChainResidueDetails
ALEU12-VAL25

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BMET631
AASN35
AASN122

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9H0U4, ECO:0000269|PubMed:27552051, ECO:0007744|PDB:5LPN, ECO:0007744|PDB:5SZJ
ChainResidueDetails
AASP64
ASER152

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by LRRK2 => ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:29562525, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:30398148, ECO:0000269|PubMed:30635421
ChainResidueDetails
ATHR73

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS102

site_idSWS_FT_FI5
Number of Residues2
DetailsLIPID: S-geranylgeranyl cysteine => ECO:0000250
ChainResidueDetails
ACYS199
ACYS200

site_idSWS_FT_FI6
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:31540829
ChainResidueDetails
ALYS102
ALYS136
ALYS154

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PDB entries from 2024-10-16

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