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1ZCB

Crystal structure of G alpha 13 in complex with GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001525biological_processangiogenesis
A0001569biological_processbranching involved in blood vessel morphogenesis
A0001664molecular_functionG protein-coupled receptor binding
A0001701biological_processin utero embryonic development
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005834cellular_componentheterotrimeric G-protein complex
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0007204biological_processpositive regulation of cytosolic calcium ion concentration
A0007266biological_processRho protein signal transduction
A0008217biological_processregulation of blood pressure
A0008360biological_processregulation of cell shape
A0010762biological_processregulation of fibroblast migration
A0016020cellular_componentmembrane
A0019001molecular_functionguanyl nucleotide binding
A0030154biological_processcell differentiation
A0030168biological_processplatelet activation
A0030334biological_processregulation of cell migration
A0031526cellular_componentbrush border membrane
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0031752molecular_functionD5 dopamine receptor binding
A0035556biological_processintracellular signal transduction
A0042470cellular_componentmelanosome
A0046872molecular_functionmetal ion binding
A0098794cellular_componentpostsynapse
A0150052biological_processregulation of postsynapse assembly
A0160221biological_processRho-activating G protein-coupled receptor signaling pathway
A1904706biological_processnegative regulation of vascular associated smooth muscle cell proliferation
A1904753biological_processnegative regulation of vascular associated smooth muscle cell migration
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP A 378
ChainResidue
AGLU58
AARG200
AASN291
ALYS292
AASP294
ALEU295
ATHR348
AALA349
AILE350
AHOH386
AHOH392
ASER59
AHOH399
AHOH417
AHOH424
AGLY60
ALYS61
ASER62
ATHR63
AGLU172
ALEU197
ALEU198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues13
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsRegion: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16388592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18940608","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZCB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18940608","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CX6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18940608","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CX7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q14344","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bh2
ChainResidueDetails
AGLU58
AARG200
ATHR203

246031

PDB entries from 2025-12-10

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