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4F5Y

Crystal structure of human STING CTD complex with C-di-GMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0002218biological_processactivation of innate immune response
A0032481biological_processpositive regulation of type I interferon production
B0002218biological_processactivation of innate immune response
B0032481biological_processpositive regulation of type I interferon production
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP205
AGLU316
AHOH570
BVAL341
BHOH639
BHOH640

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE C2E A 402
ChainResidue
AVAL239
ATHR263
APRO264
AHOH516
AHOH520
AHOH571
BSER162
BGLY166
BTYR167
BARG238
BTYR240
BGLU260
BTHR263
BPRO264
BHOH612
BHOH615
BHOH634
ASER162
ATYR167
AARG238

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 500
ChainResidue
AVAL341
BASP205
BGLU316

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22728660, ECO:0007744|PDB:4F5Y
ChainResidueDetails
ASER162
BSER162

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22579474, ECO:0000269|PubMed:22705373, ECO:0000269|PubMed:22728658, ECO:0000269|PubMed:22728659, ECO:0000269|PubMed:22728660, ECO:0007744|PDB:4EF4, ECO:0007744|PDB:4EMT, ECO:0007744|PDB:4F5D, ECO:0007744|PDB:4F5Y, ECO:0007744|PDB:4F9G
ChainResidueDetails
ATYR167
BTYR167

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:37379839, ECO:0007744|PDB:8GJX
ChainResidueDetails
AARG238
BARG238

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22579474, ECO:0000269|PubMed:22705373, ECO:0000269|PubMed:22728658, ECO:0000269|PubMed:22728660, ECO:0007744|PDB:4EF4, ECO:0007744|PDB:4EMT, ECO:0007744|PDB:4F5Y, ECO:0007744|PDB:4F9G
ChainResidueDetails
ATHR263
BTHR263

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:37832545
ChainResidueDetails
ATHR229
ATHR354
ATHR356
BTHR229
BTHR354
BTHR356

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:37832545
ChainResidueDetails
ASER241
BSER241

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine; by MAP3K7 => ECO:0000269|PubMed:37832545
ChainResidueDetails
ASER355
BSER355

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by TBK1 => ECO:0000269|PubMed:18818105, ECO:0000269|PubMed:25636800
ChainResidueDetails
ASER358
BSER358

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine; by TBK1 => ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:27302953, ECO:0000269|PubMed:32753499
ChainResidueDetails
ASER366
BSER366

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19285439, ECO:0000269|PubMed:21074459
ChainResidueDetails
ALYS150
BLYS150

site_idSWS_FT_FI11
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000250|UniProtKB:Q3TBT3
ChainResidueDetails
ALYS338
BLYS338

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:31968013
ChainResidueDetails
ALYS236
BLYS236

218853

PDB entries from 2024-04-24

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