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3BRW

Structure of the Rap-RapGAP complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005096molecular_functionGTPase activator activity
A0051056biological_processregulation of small GTPase mediated signal transduction
B0005096molecular_functionGTPase activator activity
B0051056biological_processregulation of small GTPase mediated signal transduction
C0005096molecular_functionGTPase activator activity
C0051056biological_processregulation of small GTPase mediated signal transduction
D0000166molecular_functionnucleotide binding
D0003924molecular_functionGTPase activity
D0003925molecular_functionG protein activity
D0005515molecular_functionprotein binding
D0005525molecular_functionGTP binding
D0005811cellular_componentlipid droplet
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0005911cellular_componentcell-cell junction
D0007165biological_processsignal transduction
D0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
D0019003molecular_functionGDP binding
D0030073biological_processinsulin secretion
D0031045cellular_componentdense core granule
D0032486biological_processRap protein signal transduction
D0033625biological_processpositive regulation of integrin activation
D0035577cellular_componentazurophil granule membrane
D0044877molecular_functionprotein-containing complex binding
D0045121cellular_componentmembrane raft
D0061028biological_processestablishment of endothelial barrier
D0070062cellular_componentextracellular exosome
D0070161cellular_componentanchoring junction
D0071320biological_processcellular response to cAMP
D0098978cellular_componentglutamatergic synapse
D0099010biological_processmodification of postsynaptic structure
D1901888biological_processregulation of cell junction assembly
D2000114biological_processregulation of establishment of cell polarity
D2000301biological_processnegative regulation of synaptic vesicle exocytosis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 172
ChainResidue
DSER17
DTHR35
DHOH174
DHOH175

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BEF D 170
ChainResidue
DPRO34
DTHR35
DGLY60
DHOH175
BASN290
DGLY12
DGLY13
DLYS16
DTYR32

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GDP D 171
ChainResidue
BGLN280
DGLY13
DGLY15
DLYS16
DSER17
DALA18
DGLU30
DLYS31
DTYR32
DASN116
DLYS117
DASP119
DLEU120
DSER147
DALA148
DLYS149
DHOH174
DHOH175

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues432
DetailsDomain: {"description":"Rap-GAP","evidences":[{"source":"PROSITE-ProRule","id":"PRU00165","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues42
DetailsRegion: {"description":"Interaction with KRIT1","evidences":[{"source":"PubMed","id":"22577140","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsMotif: {"description":"Effector region","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues17
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18309292","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22577140","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylserine; by botulinum toxin","evidences":[{"source":"PubMed","id":"3141412","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
DTHR61

249697

PDB entries from 2026-02-25

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