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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7FU4

Crystal Structure of human cyclic GMP-AMP synthase in complex with 2-[(2-fluoro-4-phenylphenyl)methylamino]-5-propyl-4H-[1,2,4]triazolo[1,5-a]pyrimidin-7-one

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q8C6L5

Chain	Residue	Details
A	THR211

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:30007416, ECO:0007744\|PDB:6CTA

Chain	Residue	Details
A	SER213
A	SER380
A	LYS414

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:30007416, ECO:0000305\|PubMed:23722159, ECO:0000305\|PubMed:26229115, ECO:0007744\|PDB:6CT9, ECO:0007744\|PDB:6CTA

Chain	Residue	Details
A	GLU225
A	ASP227

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:30007416, ECO:0007744\|PDB:6CT9, ECO:0007744\|PDB:6CTA

Chain	Residue	Details
A	ASP319

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:24462292, ECO:0000269\|PubMed:31113940, ECO:0007744\|PDB:4O67, ECO:0007744\|PDB:6MJX

Chain	Residue	Details
A	LYS362
A	ARG376

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: 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

Chain	Residue	Details
A	HIS390

site_id	SWS_FT_FI7
Number of Residues	3
Details	BINDING: 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

Chain	Residue	Details
A	CYS396
A	CYS397
A	CYS404

site_id	SWS_FT_FI8
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:30007416, ECO:0000305\|PubMed:24462292, ECO:0007744\|PDB:6CTA

Chain	Residue	Details
A	SER435

site_id	SWS_FT_FI9
Number of Residues	2
Details	SITE: Important for preferential detection of curved long DNA => ECO:0000269\|PubMed:30007416

Chain	Residue	Details
A	LYS187
A	LEU195

site_id	SWS_FT_FI10
Number of Residues	1
Details	SITE: Arginine-anchor => ECO:0000269\|PubMed:32911482, ECO:0000269\|PubMed:32912999, ECO:0000269\|PubMed:33051594

Chain	Residue	Details
A	ARG255

site_id	SWS_FT_FI11
Number of Residues	1
Details	SITE: Cleavage; by CASP3 => ECO:0000269\|PubMed:30878284

Chain	Residue	Details
A	ASP319

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: PolyADP-ribosyl aspartic acid => ECO:0000269\|PubMed:35460603

Chain	Residue	Details
A	ASP191

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: (Microbial infection) Deamidated asparagine; by herpes simplex virus 1/HHV-1 UL37 => ECO:0000269\|PubMed:30092200

Chain	Residue	Details
A	ASN210
A	ASN389

site_id	SWS_FT_FI14
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:33273464

Chain	Residue	Details
A	SER213

site_id	SWS_FT_FI15
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by BLK => ECO:0000269\|PubMed:30356214

Chain	Residue	Details
A	TYR215

site_id	SWS_FT_FI16
Number of Residues	1
Details	MOD_RES: 5-glutamyl polyglutamate => ECO:0000250\|UniProtKB:Q8C6L5

Chain	Residue	Details
A	GLU286

site_id	SWS_FT_FI17
Number of Residues	1
Details	MOD_RES: Phosphoserine; by CDK1 and PKB => ECO:0000269\|PubMed:26440888, ECO:0000269\|PubMed:32351706, ECO:0000269\|PubMed:33542149

Chain	Residue	Details
A	SER305

site_id	SWS_FT_FI18
Number of Residues	1
Details	MOD_RES: 5-glutamyl glutamate => ECO:0000250\|UniProtKB:Q8C6L5

Chain	Residue	Details
A	GLU314

site_id	SWS_FT_FI19
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:30799039

Chain	Residue	Details
A	LYS384
A	LYS392
A	LYS394

site_id	SWS_FT_FI20
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:30799039, ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS414

site_id	SWS_FT_FI21
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:32474700

Chain	Residue	Details
A	SER434
A	SER435

site_id	SWS_FT_FI22
Number of Residues	2
Details	MOD_RES: (Microbial infection) Deamidated glutamine; by herpes simplex virus 1/HHV-1 UL37 => ECO:0000269\|PubMed:30092200

Chain	Residue	Details
A	GLN451
A	GLN454

site_id	SWS_FT_FI23
Number of Residues	1
Details	MOD_RES: N6-methyllysine => ECO:0000269\|PubMed:35210392

Chain	Residue	Details
A	LYS506

site_id	SWS_FT_FI24
Number of Residues	2
Details	LIPID: S-palmitoyl cysteine => ECO:0000269\|PubMed:37802025

Chain	Residue	Details
A	CYS404
A	CYS405

site_id	SWS_FT_FI25
Number of Residues	1
Details	LIPID: S-palmitoyl cysteine => ECO:0000269\|PubMed:35438208

Chain	Residue	Details
A	CYS474

site_id	SWS_FT_FI26
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:28273161

Chain	Residue	Details
A	LYS173

site_id	SWS_FT_FI27
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:27637147

Chain	Residue	Details
A	LYS479

site_id	SWS_FT_FI28
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269\|PubMed:27637147

Chain	Residue	Details
A	LYS231

site_id	SWS_FT_FI29
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:27637147

Chain	Residue	Details
A	LYS285

site_id	SWS_FT_FI30
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250\|UniProtKB:Q8C6L5

Chain	Residue	Details
A	LYS347

site_id	SWS_FT_FI31
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:28273161

Chain	Residue	Details
A	LYS384

site_id	SWS_FT_FI32
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000250\|UniProtKB:Q8C6L5

Chain	Residue	Details
A	LYS394

site_id	SWS_FT_FI33
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:35503863

Chain	Residue	Details
A	LYS411

site_id	SWS_FT_FI34
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:27666593

Chain	Residue	Details
A	LYS414

site_id	SWS_FT_FI35
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:38418882

Chain	Residue	Details
A	LYS427
A	LYS428

229183

PDB entries from 2024-12-18

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