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7FTH

Crystal Structure of human cyclic GMP-AMP synthase in complex with cGAMP

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8C6L5
ChainResidueDetails
ATHR211

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:30007416, ECO:0007744|PDB:6CTA
ChainResidueDetails
ASER213
ASER380
ALYS414

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:30007416, ECO:0000305|PubMed:23722159, ECO:0000305|PubMed:26229115, ECO:0007744|PDB:6CT9, ECO:0007744|PDB:6CTA
ChainResidueDetails
AGLU225
AASP227

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:30007416, ECO:0007744|PDB:6CT9, ECO:0007744|PDB:6CTA
ChainResidueDetails
AASP319

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:31113940, ECO:0007744|PDB:4O67, ECO:0007744|PDB:6MJX
ChainResidueDetails
ALYS362
AARG376

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:23707061, ECO:0000269|PubMed:24332030, ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:28934246, ECO:0000269|PubMed:28940468, ECO:0000269|PubMed:30007416, ECO:0000269|PubMed:31113940, ECO:0000269|PubMed:31142647, ECO:0000269|PubMed:32911482, ECO:0000269|PubMed:32912999, ECO:0007744|PDB:5V8O, ECO:0007744|PDB:5VDO, ECO:0007744|PDB:5VDP, ECO:0007744|PDB:5VDQ, ECO:0007744|PDB:5VDR, ECO:0007744|PDB:5VDS, ECO:0007744|PDB:5VDT, ECO:0007744|PDB:5VDU, ECO:0007744|PDB:5VDV, ECO:0007744|PDB:5VDW, ECO:0007744|PDB:6CT9, ECO:0007744|PDB:6CTA, ECO:0007744|PDB:6EDB, ECO:0007744|PDB:6EDC, ECO:0007744|PDB:6MJU, ECO:0007744|PDB:6MJW, ECO:0007744|PDB:6MJX, ECO:0007744|PDB:6NAO, ECO:0007744|PDB:6NFG, ECO:0007744|PDB:6NFO, ECO:0007744|PDB:6Y5D, ECO:0007744|PDB:6Y5E, ECO:0007744|PDB:7C0M
ChainResidueDetails
AHIS390

site_idSWS_FT_FI7
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:23707061, ECO:0000269|PubMed:24332030, ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:28934246, ECO:0000269|PubMed:28940468, ECO:0000269|PubMed:30007416, ECO:0000269|PubMed:31113940, ECO:0000269|PubMed:31142647, ECO:0000269|PubMed:32459092, ECO:0000269|PubMed:32911482, ECO:0000269|PubMed:32912999, ECO:0007744|PDB:5V8O, ECO:0007744|PDB:5VDO, ECO:0007744|PDB:5VDP, ECO:0007744|PDB:5VDQ, ECO:0007744|PDB:5VDR, ECO:0007744|PDB:5VDS, ECO:0007744|PDB:5VDT, ECO:0007744|PDB:5VDU, ECO:0007744|PDB:5VDV, ECO:0007744|PDB:5VDW, ECO:0007744|PDB:6CT9, ECO:0007744|PDB:6CTA, ECO:0007744|PDB:6EDB, ECO:0007744|PDB:6EDC, ECO:0007744|PDB:6LRC, ECO:0007744|PDB:6MJU, ECO:0007744|PDB:6MJW, ECO:0007744|PDB:6MJX, ECO:0007744|PDB:6NAO, ECO:0007744|PDB:6NFG, ECO:0007744|PDB:6NFO, ECO:0007744|PDB:6O47, ECO:0007744|PDB:6Y5D, ECO:0007744|PDB:6Y5E, ECO:0007744|PDB:7C0M
ChainResidueDetails
ACYS396
ACYS397
ACYS404

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:30007416, ECO:0000305|PubMed:24462292, ECO:0007744|PDB:6CTA
ChainResidueDetails
ASER435

site_idSWS_FT_FI9
Number of Residues2
DetailsSITE: Important for preferential detection of curved long DNA => ECO:0000269|PubMed:30007416
ChainResidueDetails
ALYS187
ALEU195

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Arginine-anchor => ECO:0000269|PubMed:32911482, ECO:0000269|PubMed:32912999, ECO:0000269|PubMed:33051594
ChainResidueDetails
AARG255

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Cleavage; by CASP3 => ECO:0000269|PubMed:30878284
ChainResidueDetails
AASP319

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: PolyADP-ribosyl aspartic acid => ECO:0000269|PubMed:35460603
ChainResidueDetails
AASP191

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: (Microbial infection) Deamidated asparagine; by herpes simplex virus 1/HHV-1 UL37 => ECO:0000269|PubMed:30092200
ChainResidueDetails
AASN210
AASN389

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:33273464
ChainResidueDetails
ASER213

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by BLK => ECO:0000269|PubMed:30356214
ChainResidueDetails
ATYR215

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q8C6L5
ChainResidueDetails
AGLU286

site_idSWS_FT_FI17
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 and PKB => ECO:0000269|PubMed:26440888, ECO:0000269|PubMed:32351706, ECO:0000269|PubMed:33542149
ChainResidueDetails
ASER305

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: 5-glutamyl glutamate => ECO:0000250|UniProtKB:Q8C6L5
ChainResidueDetails
AGLU314

site_idSWS_FT_FI19
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30799039
ChainResidueDetails
ALYS384
ALYS392
ALYS394

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30799039, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS414

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:32474700
ChainResidueDetails
ASER434
ASER435

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: (Microbial infection) Deamidated glutamine; by herpes simplex virus 1/HHV-1 UL37 => ECO:0000269|PubMed:30092200
ChainResidueDetails
AGLN451
AGLN454

site_idSWS_FT_FI23
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000269|PubMed:35210392
ChainResidueDetails
ALYS506

site_idSWS_FT_FI24
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:37802025
ChainResidueDetails
ACYS404
ACYS405

site_idSWS_FT_FI25
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:35438208
ChainResidueDetails
ACYS474

site_idSWS_FT_FI26
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:28273161
ChainResidueDetails
ALYS173

site_idSWS_FT_FI27
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:27637147
ChainResidueDetails
ALYS479

site_idSWS_FT_FI28
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:27637147
ChainResidueDetails
ALYS231

site_idSWS_FT_FI29
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27637147
ChainResidueDetails
ALYS285

site_idSWS_FT_FI30
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:Q8C6L5
ChainResidueDetails
ALYS347

site_idSWS_FT_FI31
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:28273161
ChainResidueDetails
ALYS384

site_idSWS_FT_FI32
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000250|UniProtKB:Q8C6L5
ChainResidueDetails
ALYS394

site_idSWS_FT_FI33
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:35503863
ChainResidueDetails
ALYS411

site_idSWS_FT_FI34
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27666593
ChainResidueDetails
ALYS414

site_idSWS_FT_FI35
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:38418882
ChainResidueDetails
ALYS427
ALYS428

227111

PDB entries from 2024-11-06

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