Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5F9F

Crystal structure of RIG-I helicase-RD in complex with 24-mer blunt-end 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	1
Details	binding site for residue MG A 1002

Chain	Residue
A	LYS723

site_id	AC3
Number of Residues	6
Details	binding site for residue ETF A 1003

Chain	Residue
A	LEU408
A	THR409
A	ILE262
A	ALA264
A	CYS268
A	LYS270

site_id	AC4
Number of Residues	6
Details	binding site for residue BU3 A 1004

Chain	Residue
A	GLU510
A	ARG546
A	ASP550
A	TYR566
A	THR636
B	A19

site_id	AC5
Number of Residues	4
Details	binding site for residue BU3 A 1005

Chain	Residue
A	GLY269
A	LYS270
A	THR271
A	PHE272

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 BU3 C 1003

Chain	Residue
C	LYS666
C	THR667
C	ASN668
C	LYS888

site_id	AC8
Number of Residues	9
Details	binding site for residue BU3 C 1004

Chain	Residue
A	ARG320
A	GLN336
A	ILE337
A	ASN340
A	ASN341
C	ARG320
C	ILE337
C	ASN340
C	ASN341

site_id	AC9
Number of Residues	4
Details	binding site for residue BU3 C 1005

Chain	Residue
C	ASN376
C	ALA700
D	A5
D	U22

site_id	AD1
Number of Residues	6
Details	binding site for residue BU3 C 1006

Chain	Residue
C	ILE262
C	ALA264
C	CYS268
C	LYS270
C	LEU408
C	THR409

site_id	AD2
Number of Residues	4
Details	binding site for residue ZN E 1001

Chain	Residue
E	CYS810
E	CYS813
E	CYS864
E	CYS869

site_id	AD3
Number of Residues	5
Details	binding site for residue ETF E 1002

Chain	Residue
E	LYS666
E	ASN668
E	GLN669
E	ASP872
E	LYS888

site_id	AD4
Number of Residues	8
Details	binding site for residue BU3 E 1003

Chain	Residue
E	LEU250
E	ILE262
E	ALA264
E	CYS268
E	LYS270
E	VAL273
E	LEU408
E	THR409

site_id	AD5
Number of Residues	8
Details	binding site for residue BU3 E 1004

Chain	Residue
E	LEU714
E	TYR717
E	GLY719
E	ASN720
E	LYS723
E	MET724
E	THR727
E	GLU751

site_id	AD6
Number of Residues	4
Details	binding site for residue ZN G 1001

Chain	Residue
G	CYS810
G	CYS813
G	CYS864
G	CYS869

site_id	AD7
Number of Residues	8
Details	binding site for residue ETF G 1002

Chain	Residue
G	ARG320
G	ILE337
G	ASN340
G	ASN341
K	GLN336
K	ILE337
K	ASN340
K	ASN341

site_id	AD8
Number of Residues	7
Details	binding site for residue BU3 G 1003

Chain	Residue
G	ILE262
G	ALA264
G	PRO265
G	CYS268
G	LYS270
G	THR409
G	GLU702

site_id	AD9
Number of Residues	5
Details	binding site for residue BU3 G 1004

Chain	Residue
G	ALA329
G	GLU330
G	ILE350
G	ASN353
G	ASN354

site_id	AE1
Number of Residues	6
Details	binding site for residue BU3 G 1005

Chain	Residue
G	GLY719
G	LYS723
G	THR727
G	GLU751
G	LEU714
G	TYR717

site_id	AE2
Number of Residues	4
Details	binding site for residue ZN I 1001

Chain	Residue
I	CYS810
I	CYS813
I	CYS864
I	CYS869

site_id	AE3
Number of Residues	1
Details	binding site for residue MG I 1003

Chain	Residue
I	LYS723

site_id	AE4
Number of Residues	6
Details	binding site for residue BU3 I 1004

Chain	Residue
I	ILE262
I	ALA264
I	CYS268
I	LYS270
I	LEU408
I	THR409

site_id	AE5
Number of Residues	4
Details	binding site for residue ZN K 1001

Chain	Residue
K	CYS810
K	CYS813
K	CYS864
K	CYS869

site_id	AE6
Number of Residues	1
Details	binding site for residue MG K 1002

Chain	Residue
K	LYS723

site_id	AE7
Number of Residues	5
Details	binding site for residue ETF K 1003

Chain	Residue
K	PRO456
K	LYS458
K	THR727
K	ARG728
K	CYS738

site_id	AE8
Number of Residues	6
Details	binding site for residue BU3 K 1004

Chain	Residue
K	ILE262
K	ALA264
K	CYS268
K	LYS270
K	LEU408
K	THR409

Functional Information from SwissProt/UniProt

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

Chain	Residue	Details
A	VAL309
C	VAL309
E	VAL309
G	VAL309
I	VAL309
K	VAL309

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

Chain	Residue	Details
A	SER855
E	LYS858
E	LYS909
E	GLU914
G	SER855
G	LYS858
G	LYS909
G	GLU914
I	SER855
I	LYS858
I	LYS909
A	LYS858
I	GLU914
K	SER855
K	LYS858
K	LYS909
K	GLU914
A	LYS909
A	GLU914
C	SER855
C	LYS858
C	LYS909
C	GLU914
E	SER855

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	LEU540
I	LEU594
K	LEU540
K	LEU594
A	LEU594
C	LEU540
C	LEU594
E	LEU540
E	LEU594
G	LEU540
G	LEU594
I	LEU540

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

Chain	Residue	Details
A	ALA815
C	ALA815
E	ALA815
G	ALA815
I	ALA815
K	ALA815

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

Chain	Residue	Details
A	THR899
I	GLY900
K	THR899
K	GLY900
A	GLY900
C	THR899
C	GLY900
E	THR899
E	GLY900
G	THR899
G	GLY900
I	THR899

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

Chain	Residue	Details
A	THR903
C	THR903
E	THR903
G	THR903
I	THR903
K	THR903

site_id	SWS_FT_FI7
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	GLU857
K	GLU857
C	GLU857
E	GLU857
G	GLU857
I	GLU857

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