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4HDO

Crystal structure of the binary Complex of KRIT1 bound to the Rap1 GTPase

Functional Information from GO Data
ChainGOidnamespacecontents
B0000166molecular_functionnucleotide binding
B0003924molecular_functionGTPase activity
B0003925molecular_functionG protein activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005811cellular_componentlipid droplet
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005911cellular_componentcell-cell junction
B0007165biological_processsignal transduction
B0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0019003molecular_functionGDP binding
B0030073biological_processinsulin secretion
B0031045cellular_componentdense core granule
B0032486biological_processRap protein signal transduction
B0033625biological_processpositive regulation of integrin activation
B0035577cellular_componentazurophil granule membrane
B0044877molecular_functionprotein-containing complex binding
B0045121cellular_componentmembrane raft
B0061028biological_processestablishment of endothelial barrier
B0070062cellular_componentextracellular exosome
B0070161cellular_componentanchoring junction
B0071320biological_processcellular response to cAMP
B0098978cellular_componentglutamatergic synapse
B0099010biological_processmodification of postsynaptic structure
B1901888biological_processregulation of cell junction assembly
B2000114biological_processregulation of establishment of cell polarity
B2000301biological_processnegative regulation of synaptic vesicle exocytosis
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 801
ChainResidue
ASER471
APHE639
AHOH934

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 200
ChainResidue
BSER17
BTHR35
BGNP201
BHOH385
BHOH386

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE GNP B 201
ChainResidue
BVAL14
BGLY15
BLYS16
BSER17
BALA18
BPHE28
BVAL29
BGLU30
BTYR32
BPRO34
BTHR35
BGLY60
BASN116
BLYS117
BASP119
BLEU120
BSER147
BALA148
BLYS149
BMG200
BHOH305
BHOH313
BHOH384
BHOH385
BHOH386
BGLY13

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsRegion: {"description":"Interaction with RAP1B","evidences":[{"source":"PubMed","id":"22577140","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsMotif: {"description":"Effector region","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues17
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18309292","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22577140","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylserine; by botulinum toxin","evidences":[{"source":"PubMed","id":"3141412","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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