Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6Y5E

Structure of human cGAS (K394E) bound to the nucleosome (focused refinement of cGAS-NCP subcomplex)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
A	0030527	molecular_function	structural constituent of chromatin
A	0046982	molecular_function	protein heterodimerization activity
B	0003677	molecular_function	DNA binding
B	0030527	molecular_function	structural constituent of chromatin
B	0046982	molecular_function	protein heterodimerization activity
C	0000786	cellular_component	nucleosome
C	0003677	molecular_function	DNA binding
C	0030527	molecular_function	structural constituent of chromatin
C	0046982	molecular_function	protein heterodimerization activity
D	0000786	cellular_component	nucleosome
D	0003677	molecular_function	DNA binding
D	0030527	molecular_function	structural constituent of chromatin
D	0046982	molecular_function	protein heterodimerization activity
E	0000786	cellular_component	nucleosome
E	0003677	molecular_function	DNA binding
E	0030527	molecular_function	structural constituent of chromatin
E	0046982	molecular_function	protein heterodimerization activity
F	0003677	molecular_function	DNA binding
F	0030527	molecular_function	structural constituent of chromatin
F	0046982	molecular_function	protein heterodimerization activity
G	0000786	cellular_component	nucleosome
G	0003677	molecular_function	DNA binding
G	0030527	molecular_function	structural constituent of chromatin
G	0046982	molecular_function	protein heterodimerization activity
H	0000786	cellular_component	nucleosome
H	0003677	molecular_function	DNA binding
H	0030527	molecular_function	structural constituent of chromatin
H	0046982	molecular_function	protein heterodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue PTD A 201

Chain	Residue
A	LYS80
B	LYS80

site_id	AC2
Number of Residues	2
Details	binding site for residue PTD C 201

Chain	Residue
C	LYS100
G	LYS100

site_id	AC3
Number of Residues	2
Details	binding site for residue PTD D 301

Chain	Residue
D	LYS86
G	LYS37

site_id	AC4
Number of Residues	2
Details	binding site for residue PTD E 201

Chain	Residue
A	LYS116
E	LYS123

site_id	AC5
Number of Residues	2
Details	binding site for residue PTD E 202

Chain	Residue
E	LYS116
A	LYS123

site_id	AC6
Number of Residues	2
Details	binding site for residue PTD F 201

Chain	Residue
E	LYS80
F	LYS80

site_id	AC7
Number of Residues	2
Details	binding site for residue PTD H 301

Chain	Residue
C	LYS37
H	LYS86

site_id	AC8
Number of Residues	7
Details	binding site for Di-peptide PTD K 602 and LYS K 355

Chain	Residue
G	ARG72
G	LYS75
K	TRP330
K	LEU352
K	ARG353
K	LEU354
K	PRO356

Functional Information from PROSITE/UniProt

site_id	PS00046
Number of Residues	7
Details	HISTONE_H2A Histone H2A signature. AGLqFPV

Chain	Residue	Details
C	ALA22-VAL28
G	ALA22-VAL28

site_id	PS00959
Number of Residues	9
Details	HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI

Chain	Residue	Details
A	PRO67-ILE75

site_id	PS00357
Number of Residues	23
Details	HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG

Chain	Residue	Details
D	ARG93-GLY115
H	ARG93-GLY115

Functional Information from SwissProt/UniProt

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

Chain	Residue	Details
K	THR211
H	LYS117
H	LYS121

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

Chain	Residue	Details
K	SER213
K	SER380
K	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
K	GLU225
K	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
K	ASP319
H	LYS86

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
K	LYS362
K	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
K	HIS390
E	THR81

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
K	CYS396
K	CYS397
K	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
K	SER435
H	ARG93

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
K	LYS187
K	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
K	ARG255
F	LYS60
F	LYS80

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

Chain	Residue	Details
K	ASP319
F	LYS92

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

Chain	Residue	Details
K	ASP191
H	LYS121

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
K	ASN210
K	ASN389

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

Chain	Residue	Details
K	SER213

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

Chain	Residue	Details
K	TYR215

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

Chain	Residue	Details
K	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
K	SER305

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

Chain	Residue	Details
K	GLU314

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

Chain	Residue	Details
K	LYS384
K	LYS392
K	GLU394

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
K	LYS414

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

Chain	Residue	Details
K	SER434
K	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
K	GLN451
K	GLN454

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

Chain	Residue	Details
K	LYS506

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

Chain	Residue	Details
K	CYS404
K	CYS405

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

Chain	Residue	Details
K	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
K	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
K	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
K	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
K	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
K	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
K	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
K	GLU394

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
K	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
K	LYS414

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)