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2F9M

3D structure of active human Rab11b GTPase

Functional Information from GO Data
ChainGOidnamespacecontents
A0001881biological_processreceptor recycling
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0008021cellular_componentsynaptic vesicle
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019003molecular_functionGDP binding
A0030670cellular_componentphagocytic vesicle membrane
A0030672cellular_componentsynaptic vesicle membrane
A0031489molecular_functionmyosin V binding
A0032402biological_processmelanosome transport
A0032456biological_processendocytic recycling
A0033572biological_processtransferrin transport
A0035773biological_processinsulin secretion involved in cellular response to glucose stimulus
A0044070biological_processregulation of monoatomic anion transport
A0045054biological_processconstitutive secretory pathway
A0045055biological_processregulated exocytosis
A0045202cellular_componentsynapse
A0045296molecular_functioncadherin binding
A0045335cellular_componentphagocytic vesicle
A0055037cellular_componentrecycling endosome
A0055038cellular_componentrecycling endosome membrane
A0070062cellular_componentextracellular exosome
A0071468biological_processcellular response to acidic pH
A0090150biological_processestablishment of protein localization to membrane
A0150093biological_processamyloid-beta clearance by transcytosis
A2000008biological_processregulation of protein localization to cell surface
A2001135biological_processregulation of endocytic recycling
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1201
ChainResidue
ASER25
ATHR43
AGNP1200
AHOH1211
AHOH1220

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI A 1202
ChainResidue
AHOH1300
AHOH1348
AGLU108
AHIS112
AHOH1264
AHOH1281

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI A 1203
ChainResidue
AMET7
AASP183
AHIS187
AHOH1247
AHOH1483

site_idAC4
Number of Residues30
DetailsBINDING SITE FOR RESIDUE GNP A 1200
ChainResidue
ASER20
AGLY21
AVAL22
AGLY23
ALYS24
ASER25
AASN26
APHE36
AASN37
ALEU38
ASER40
ASER42
ATHR43
AALA68
AGLY69
AASN124
ALYS125
AASP127
ALEU128
ASER154
AALA155
ALEU156
AMG1201
AHOH1211
AHOH1220
AHOH1221
AHOH1245
AHOH1282
AHOH1344
AHOH1464

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VVLiGDSGVGKsnL
ChainResidueDetails
AVAL14-LEU27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16545962
ChainResidueDetails
AGLY18
AASP66
AASN124
ASER154

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AGLN70

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AGLY21

225158

PDB entries from 2024-09-18

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