Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5F9H

Crystal structure of RIG-I helicase-RD in complex with 24-mer 5' triphosphate hairpin RNA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0005524	molecular_function	ATP binding
C	0003676	molecular_function	nucleic acid binding
C	0005524	molecular_function	ATP binding
E	0003676	molecular_function	nucleic acid binding
E	0005524	molecular_function	ATP binding
G	0003676	molecular_function	nucleic acid binding
G	0005524	molecular_function	ATP binding
I	0003676	molecular_function	nucleic acid binding
I	0005524	molecular_function	ATP binding
K	0003676	molecular_function	nucleic acid binding
K	0005524	molecular_function	ATP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 1001

Chain	Residue
A	CYS810
A	CYS813
A	CYS864
A	CYS869

site_id	AC2
Number of Residues	4
Details	binding site for residue MG A 1002

Chain	Residue
A	PHE285
A	PRO286
A	GLN287
A	GLN289

site_id	AC3
Number of Residues	3
Details	binding site for residue MG A 1003

Chain	Residue
A	PRO382
B	A3
A	GLN349

site_id	AC4
Number of Residues	1
Details	binding site for residue MG A 1004

Chain	Residue
A	LYS270

site_id	AC5
Number of Residues	11
Details	binding site for residue GTP B 101

Chain	Residue
A	ARG664
A	HIS830
A	HIS847
A	PHE853
A	LYS858
A	LYS861
A	ASP872
A	ILE875
A	LYS888
B	A2
B	C24

site_id	AC6
Number of Residues	4
Details	binding site for residue ZN C 1001

Chain	Residue
C	CYS810
C	CYS813
C	CYS864
C	CYS869

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN E 1001

Chain	Residue
E	CYS810
E	CYS813
E	CYS864
E	CYS869

site_id	AC8
Number of Residues	2
Details	binding site for residue MG E 1002

Chain	Residue
E	ASN376
F	A5

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN G 1001

Chain	Residue
G	CYS810
G	CYS813
G	CYS864
G	CYS869

site_id	AD1
Number of Residues	2
Details	binding site for residue MG G 1002

Chain	Residue
G	THR636
G	LEU639

site_id	AD2
Number of Residues	2
Details	binding site for residue MG G 1003

Chain	Residue
G	ASN341
K	ASN341

site_id	AD3
Number of Residues	4
Details	binding site for residue ZN I 1001

Chain	Residue
I	CYS810
I	CYS813
I	CYS864
I	CYS869

site_id	AD4
Number of Residues	2
Details	binding site for residue MG I 1002

Chain	Residue
E	ASN341
I	ASN341

site_id	AD5
Number of Residues	4
Details	binding site for residue ZN K 1001

Chain	Residue
K	CYS810
K	CYS813
K	CYS864
K	CYS869

site_id	AD6
Number of Residues	3
Details	binding site for residue MG K 1002

Chain	Residue
K	PHE285
K	PRO286
K	GLN289

site_id	AD7
Number of Residues	13
Details	binding site for Di-nucleotide GTP D 101 and A D 2

Chain	Residue
C	HIS830
C	HIS847
C	PHE853
C	LYS858
C	LYS861
C	ASP872
C	ILE875
C	VAL886
C	LYS888
C	TRP908
D	A3
D	U23
D	C24

site_id	AD8
Number of Residues	13
Details	binding site for Di-nucleotide GTP F 101 and A F 2

Chain	Residue
E	HIS830
E	HIS847
E	LYS851
E	PHE853
E	LYS858
E	LYS861
E	ILE875
E	VAL886
E	LYS888
E	TRP908
F	A3
F	U23
F	C24

site_id	AD9
Number of Residues	12
Details	binding site for Di-nucleotide GTP H 101 and A H 2

Chain	Residue
G	HIS830
G	HIS847
G	PHE853
G	LYS858
G	LYS861
G	ASP872
G	ILE875
G	LYS888
G	TRP908
H	A3
H	U23
H	C24

site_id	AE1
Number of Residues	13
Details	binding site for Di-nucleotide GTP J 101 and A J 2

Chain	Residue
I	VAL886
I	LYS888
I	TRP908
J	A3
J	U23
J	C24
I	HIS830
I	HIS847
I	PHE853
I	LYS858
I	LYS861
I	ASP872
I	ILE875

site_id	AE2
Number of Residues	12
Details	binding site for Di-nucleotide GTP L 101 and A L 2

Chain	Residue
K	HIS830
K	HIS847
K	PHE853
K	LYS858
K	LYS861
K	ASP872
K	ILE875
K	LYS888
K	TRP908
L	A3
L	U23
L	C24

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	ALA264
C	ALA264
E	ALA264
G	ALA264
I	ALA264
K	ALA264

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01125

Chain	Residue	Details
A	CYS810
E	CYS813
E	CYS864
E	CYS869
G	CYS810
G	CYS813
G	CYS864
G	CYS869
I	CYS810
I	CYS813
I	CYS864
A	CYS813
I	CYS869
K	CYS810
K	CYS813
K	CYS864
K	CYS869
A	CYS864
A	CYS869
C	CYS810
C	CYS813
C	CYS864
C	CYS869
E	CYS810

site_id	SWS_FT_FI3
Number of Residues	12
Details	MOD_RES: (Microbial infection) Deamidated asparagine; by herpes simplex virus 1/HHV-1 UL37 => ECO:0000269\|PubMed:27866900

Chain	Residue	Details
A	ASN495
I	ASN549
K	ASN495
K	ASN549
A	ASN549
C	ASN495
C	ASN549
E	ASN495
E	ASN549
G	ASN495
G	ASN549
I	ASN495

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Phosphothreonine; by CK2 => ECO:0000269\|PubMed:21068236

Chain	Residue	Details
A	THR770
C	THR770
E	THR770
G	THR770
I	THR770
K	THR770

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: Phosphoserine; by CK2 => ECO:0000269\|PubMed:21068236

Chain	Residue	Details
A	SER854
I	SER855
K	SER854
K	SER855
A	SER855
C	SER854
C	SER855
E	SER854
E	SER855
G	SER854
G	SER855
I	SER854

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS858
C	LYS858
E	LYS858
G	LYS858
I	LYS858
K	LYS858

site_id	SWS_FT_FI7
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:26746851

Chain	Residue	Details
A	LYS909
C	LYS909
E	LYS909
G	LYS909
I	LYS909
K	LYS909

site_id	SWS_FT_FI8
Number of Residues	12
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:Q6Q899

Chain	Residue	Details
A	LYS812
K	LYS812
C	LYS812
E	LYS812
G	LYS812
I	LYS812

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)