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6IF3

Complex structure of Rab35 and its effector ACAP2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005096molecular_functionGTPase activator activity
B0000281biological_processmitotic cytokinesis
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005768cellular_componentendosome
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005905cellular_componentclathrin-coated pit
B0008104biological_processprotein localization
B0010008cellular_componentendosome membrane
B0015031biological_processprotein transport
B0016197biological_processendosomal transport
B0019003molecular_functionGDP binding
B0019882biological_processantigen processing and presentation
B0030136cellular_componentclathrin-coated vesicle
B0030669cellular_componentclathrin-coated endocytic vesicle membrane
B0031175biological_processneuron projection development
B0031253cellular_componentcell projection membrane
B0032456biological_processendocytic recycling
B0036010biological_processprotein localization to endosome
B0042470cellular_componentmelanosome
B0045171cellular_componentintercellular bridge
B0045334cellular_componentclathrin-coated endocytic vesicle
B0048227biological_processplasma membrane to endosome transport
B0055038cellular_componentrecycling endosome membrane
B0070062cellular_componentextracellular exosome
B1990090biological_processcellular response to nerve growth factor stimulus
Functional Information from PDB Data
site_idAC1
Number of Residues26
Detailsbinding site for residue GTP B 201
ChainResidue
BSER17
BTYR37
BTHR40
BGLY66
BASN120
BLYS121
BASP123
BSER150
BALA151
BLYS152
BMG202
BGLY18
BHOH301
BHOH322
BHOH327
BHOH332
BHOH333
BHOH410
BHOH437
BVAL19
BGLY20
BLYS21
BSER22
BSER23
BPHE33
BGLY35

site_idAC2
Number of Residues5
Detailsbinding site for residue MG B 202
ChainResidue
BSER22
BTHR40
BGTP201
BHOH322
BHOH332

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. LLIiGDSGVGKssL
ChainResidueDetails
BLEU11-LEU24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P62820
ChainResidueDetails
BGLY15
BPHE33
BASP63
BASN120
BSER150

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by LRRK2 => ECO:0000269|PubMed:29125462, ECO:0007744|PubMed:23186163
ChainResidueDetails
BTHR72

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: O-(2-cholinephosphoryl)serine => ECO:0000305|PubMed:21822290, ECO:0000305|PubMed:22307087
ChainResidueDetails
BSER75

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: O-AMP-tyrosine => ECO:0000305|PubMed:21822290
ChainResidueDetails
BTYR77

221371

PDB entries from 2024-06-19

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