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5F9H

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0005524molecular_functionATP binding
C0003676molecular_functionnucleic acid binding
C0005524molecular_functionATP binding
E0003676molecular_functionnucleic acid binding
E0005524molecular_functionATP binding
G0003676molecular_functionnucleic acid binding
G0005524molecular_functionATP binding
I0003676molecular_functionnucleic acid binding
I0005524molecular_functionATP binding
K0003676molecular_functionnucleic acid binding
K0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1001
ChainResidue
ACYS810
ACYS813
ACYS864
ACYS869

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 1002
ChainResidue
APHE285
APRO286
AGLN287
AGLN289

site_idAC3
Number of Residues3
Detailsbinding site for residue MG A 1003
ChainResidue
APRO382
BA3
AGLN349

site_idAC4
Number of Residues1
Detailsbinding site for residue MG A 1004
ChainResidue
ALYS270

site_idAC5
Number of Residues11
Detailsbinding site for residue GTP B 101
ChainResidue
AARG664
AHIS830
AHIS847
APHE853
ALYS858
ALYS861
AASP872
AILE875
ALYS888
BA2
BC24

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN C 1001
ChainResidue
CCYS810
CCYS813
CCYS864
CCYS869

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN E 1001
ChainResidue
ECYS810
ECYS813
ECYS864
ECYS869

site_idAC8
Number of Residues2
Detailsbinding site for residue MG E 1002
ChainResidue
EASN376
FA5

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN G 1001
ChainResidue
GCYS810
GCYS813
GCYS864
GCYS869

site_idAD1
Number of Residues2
Detailsbinding site for residue MG G 1002
ChainResidue
GTHR636
GLEU639

site_idAD2
Number of Residues2
Detailsbinding site for residue MG G 1003
ChainResidue
GASN341
KASN341

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN I 1001
ChainResidue
ICYS810
ICYS813
ICYS864
ICYS869

site_idAD4
Number of Residues2
Detailsbinding site for residue MG I 1002
ChainResidue
EASN341
IASN341

site_idAD5
Number of Residues4
Detailsbinding site for residue ZN K 1001
ChainResidue
KCYS810
KCYS813
KCYS864
KCYS869

site_idAD6
Number of Residues3
Detailsbinding site for residue MG K 1002
ChainResidue
KPHE285
KPRO286
KGLN289

site_idAD7
Number of Residues13
Detailsbinding site for Di-nucleotide GTP D 101 and A D 2
ChainResidue
CHIS830
CHIS847
CPHE853
CLYS858
CLYS861
CASP872
CILE875
CVAL886
CLYS888
CTRP908
DA3
DU23
DC24

site_idAD8
Number of Residues13
Detailsbinding site for Di-nucleotide GTP F 101 and A F 2
ChainResidue
EHIS830
EHIS847
ELYS851
EPHE853
ELYS858
ELYS861
EILE875
EVAL886
ELYS888
ETRP908
FA3
FU23
FC24

site_idAD9
Number of Residues12
Detailsbinding site for Di-nucleotide GTP H 101 and A H 2
ChainResidue
GHIS830
GHIS847
GPHE853
GLYS858
GLYS861
GASP872
GILE875
GLYS888
GTRP908
HA3
HU23
HC24

site_idAE1
Number of Residues13
Detailsbinding site for Di-nucleotide GTP J 101 and A J 2
ChainResidue
IVAL886
ILYS888
ITRP908
JA3
JU23
JC24
IHIS830
IHIS847
IPHE853
ILYS858
ILYS861
IASP872
IILE875

site_idAE2
Number of Residues12
Detailsbinding site for Di-nucleotide GTP L 101 and A L 2
ChainResidue
KHIS830
KHIS847
KPHE853
KLYS858
KLYS861
KASP872
KILE875
KLYS888
KTRP908
LA3
LU23
LC24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AALA264
CALA264
EALA264
GALA264
IALA264
KALA264

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01125
ChainResidueDetails
ACYS810
ECYS813
ECYS864
ECYS869
GCYS810
GCYS813
GCYS864
GCYS869
ICYS810
ICYS813
ICYS864
ACYS813
ICYS869
KCYS810
KCYS813
KCYS864
KCYS869
ACYS864
ACYS869
CCYS810
CCYS813
CCYS864
CCYS869
ECYS810

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
AASN495
IASN549
KASN495
KASN549
AASN549
CASN495
CASN549
EASN495
EASN549
GASN495
GASN549
IASN495

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphothreonine; by CK2 => ECO:0000269|PubMed:21068236
ChainResidueDetails
ATHR770
CTHR770
ETHR770
GTHR770
ITHR770
KTHR770

site_idSWS_FT_FI5
Number of Residues12
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:21068236
ChainResidueDetails
ASER854
ISER855
KSER854
KSER855
ASER855
CSER854
CSER855
ESER854
ESER855
GSER854
GSER855
ISER854

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS858
CLYS858
ELYS858
GLYS858
ILYS858
KLYS858

site_idSWS_FT_FI7
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q6Q899
ChainResidueDetails
ALYS812
KLYS812
CLYS812
ELYS812
GLYS812
ILYS812

224004

PDB entries from 2024-08-21

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