Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6TYL

Crystal structure of mammalian Ric-8A:Galpha(i):nanobody complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001965molecular_functionG-protein alpha-subunit binding
A0005085molecular_functionguanyl-nucleotide exchange factor activity
A0005096molecular_functionGTPase activator activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0005938cellular_componentcell cortex
A0006457biological_processprotein folding
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0044183molecular_functionprotein folding chaperone
B0000287molecular_functionmagnesium ion binding
B0001664molecular_functionG protein-coupled receptor binding
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0005938cellular_componentcell cortex
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
B0009898cellular_componentcytoplasmic side of plasma membrane
B0016020cellular_componentmembrane
B0019001molecular_functionguanyl nucleotide binding
B0019003molecular_functionGDP binding
B0030496cellular_componentmidbody
B0031683molecular_functionG-protein beta/gamma-subunit complex binding
B0031821molecular_functionG protein-coupled serotonin receptor binding
B0032794molecular_functionGTPase activating protein binding
B0032991cellular_componentprotein-containing complex
B0050805biological_processnegative regulation of synaptic transmission
B0051301biological_processcell division
B0060236biological_processregulation of mitotic spindle organization
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
B0099645biological_processneurotransmitter receptor localization to postsynaptic specialization membrane
B1904322biological_processcellular response to forskolin
B1904778biological_processpositive regulation of protein localization to cell cortex
F0001965molecular_functionG-protein alpha-subunit binding
F0005085molecular_functionguanyl-nucleotide exchange factor activity
F0005096molecular_functionGTPase activator activity
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0005886cellular_componentplasma membrane
F0005938cellular_componentcell cortex
F0006457biological_processprotein folding
F0007186biological_processG protein-coupled receptor signaling pathway
F0016020cellular_componentmembrane
F0044183molecular_functionprotein folding chaperone
G0000287molecular_functionmagnesium ion binding
G0001664molecular_functionG protein-coupled receptor binding
G0003924molecular_functionGTPase activity
G0005515molecular_functionprotein binding
G0005525molecular_functionGTP binding
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005813cellular_componentcentrosome
G0005834cellular_componentheterotrimeric G-protein complex
G0005886cellular_componentplasma membrane
G0005938cellular_componentcell cortex
G0007165biological_processsignal transduction
G0007186biological_processG protein-coupled receptor signaling pathway
G0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
G0009898cellular_componentcytoplasmic side of plasma membrane
G0016020cellular_componentmembrane
G0019001molecular_functionguanyl nucleotide binding
G0019003molecular_functionGDP binding
G0030496cellular_componentmidbody
G0031683molecular_functionG-protein beta/gamma-subunit complex binding
G0031821molecular_functionG protein-coupled serotonin receptor binding
G0032794molecular_functionGTPase activating protein binding
G0032991cellular_componentprotein-containing complex
G0050805biological_processnegative regulation of synaptic transmission
G0051301biological_processcell division
G0060236biological_processregulation of mitotic spindle organization
G0098794cellular_componentpostsynapse
G0098978cellular_componentglutamatergic synapse
G0099645biological_processneurotransmitter receptor localization to postsynaptic specialization membrane
G1904322biological_processcellular response to forskolin
G1904778biological_processpositive regulation of protein localization to cell cortex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"PubMed","id":"29844055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32103024","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32126208","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by CK2","evidences":[{"source":"PubMed","id":"29844055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32103024","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32126208","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q3TIR3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues26
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues18
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues14
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues10
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1AS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FFA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N0D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25037222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9705312","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1AS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FFA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N0D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 533
ChainResidueDetails
HLYS43electrostatic stabiliser
HVAL48electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 533
ChainResidueDetails
ILYS43electrostatic stabiliser
IVAL48electrostatic stabiliser

251801

PDB entries from 2026-04-08

PDB statisticsPDBj update infoContact PDBjnumon