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2F9L

3D structure of inactive human Rab11b GTPase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001881biological_processreceptor recycling
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0008021cellular_componentsynaptic vesicle
A0015031biological_processprotein transport
A0016787molecular_functionhydrolase activity
A0019003molecular_functionGDP binding
A0030670cellular_componentphagocytic vesicle membrane
A0030672cellular_componentsynaptic vesicle membrane
A0031410cellular_componentcytoplasmic vesicle
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
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
A0098876biological_processvesicle-mediated transport to the plasma membrane
A0150093biological_processamyloid-beta clearance by transcytosis
A1902017biological_processregulation of cilium assembly
A2000008biological_processregulation of protein localization to cell surface
A2001135biological_processregulation of endocytic recycling
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1175
ChainResidue
ASER25
AGDP1174
AHOH1296
AHOH1297
AHOH1298
AHOH1299

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE GDP A 1174
ChainResidue
ALYS24
ASER25
AASN26
APHE36
AASN37
ALEU38
AASN124
ALYS125
AASP127
ASER154
AALA155
ALEU156
AMG1175
AHOH1190
AHOH1201
AHOH1216
AHOH1222
AHOH1240
AHOH1241
AHOH1296
AHOH1298
AHOH1299
AGLY21
AVAL22
AGLY23

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 Residues19
DetailsMotif: {"description":"Switch 2","evidences":[{"source":"PubMed","id":"16545962","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2F9L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2F9M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16545962","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2F9M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16545962","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2F9L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2F9M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16545962","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2F9M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

246704

PDB entries from 2025-12-24

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