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6KYV

Crystal Structure of RIG-I and hairpin RNA with G-U wobble base pairs

Functional Information from GO Data
ChainGOidnamespacecontents
B0003676molecular_functionnucleic acid binding
B0005524molecular_functionATP binding
D0003676molecular_functionnucleic acid binding
D0005524molecular_functionATP binding
F0003676molecular_functionnucleic acid binding
F0005524molecular_functionATP binding
H0003676molecular_functionnucleic acid binding
H0005524molecular_functionATP binding
J0003676molecular_functionnucleic acid binding
J0005524molecular_functionATP binding
L0003676molecular_functionnucleic acid binding
L0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN B 1001
ChainResidue
BCYS810
BCYS813
BCYS864
BCYS869

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN D 1001
ChainResidue
DCYS810
DCYS813
DCYS864
DCYS869

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN F 1001
ChainResidue
FCYS813
FCYS864
FCYS869
FCYS810

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN H 1001
ChainResidue
HCYS810
HCYS813
HCYS864
HCYS869

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN J 1001
ChainResidue
JCYS810
JCYS813
JCYS864
JCYS869

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN L 1001
ChainResidue
LCYS810
LCYS813
LCYS864
LCYS869

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
BALA264
DALA264
FALA264
HALA264
JALA264
LALA264

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01125
ChainResidueDetails
BCYS810
BCYS813
BCYS864
BCYS869
DCYS810
DCYS813
DCYS864
DCYS869
FCYS810
FCYS813
FCYS864
FCYS869
HCYS810
HCYS813
HCYS864
HCYS869
JCYS810
JCYS813
JCYS864
JCYS869
LCYS810
LCYS813
LCYS864
LCYS869

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: (Microbial infection) Deamidated asparagine; by herpes simplex virus 1/HHV-1 UL37 => ECO:0000269|PubMed:27866900
ChainResidueDetails
BASN495
BASN549
DASN495
DASN549
FASN495
FASN549
HASN495
HASN549
JASN495
JASN549
LASN495
LASN549

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphothreonine; by CK2 => ECO:0000269|PubMed:21068236
ChainResidueDetails
BTHR770
DTHR770
FTHR770
HTHR770
JTHR770
LTHR770

site_idSWS_FT_FI5
Number of Residues12
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:21068236
ChainResidueDetails
BSER854
BSER855
DSER854
DSER855
FSER854
FSER855
HSER854
HSER855
JSER854
JSER855
LSER854
LSER855

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS858
DLYS858
FLYS858
HLYS858
JLYS858
LLYS858

site_idSWS_FT_FI7
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q6Q899
ChainResidueDetails
HLYS812
JLYS812
LLYS812
BLYS812
DLYS812
FLYS812

219869

PDB entries from 2024-05-15

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