Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5KQS

Structure of NS5 methyltransferase from Zika virus bound to S-adenosylmethionine and 7-methyl-guanosine-5'-diphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004482molecular_functionmRNA 5'-cap (guanine-N7-)-methyltransferase activity
A0004483molecular_functionmRNA (nucleoside-2'-O-)-methyltransferase activity
A0008168molecular_functionmethyltransferase activity
A0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue M7G A 301
ChainResidue
ALYS13
AARG213
ASER215
AGOL303
AHOH406
AHOH415
AHOH416
AHOH419
AHOH449
AHOH558
ALEU16
AASN17
AMET19
APHE24
ALYS28
ASER150
ASER151
ASER152

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 302
ChainResidue
AARG37
AARG41
ASER56
AARG57
AARG84

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 303
ChainResidue
AASN17
ASER152
AM7G301
AACT306

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 304
ChainResidue
AASP131
APHE133
AARG163
AALA265
ASAM307
AHOH409
AHOH414

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 305
ChainResidue
ATYR119
ASER261
AHOH435
AHOH447
AHOH577

site_idAC6
Number of Residues4
Detailsbinding site for residue ACT A 306
ChainResidue
ASER151
ASER152
AGOL303
AHOH443

site_idAC7
Number of Residues21
Detailsbinding site for residue SAM A 307
ChainResidue
ASER56
AGLY58
AGLY81
ACYS82
AGLY83
AGLY86
ATRP87
ATHR104
ALYS105
AVAL130
AASP131
AVAL132
APHE133
AASP146
AGOL304
APO4308
AHOH409
AHOH433
AHOH452
AHOH511
AHOH583

site_idAC8
Number of Residues6
Detailsbinding site for residue PO4 A 308
ChainResidue
AGLY109
AHIS110
AGLU111
ASAM307
AHOH403
AHOH556

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: For 2'-O-MTase activity => ECO:0000250|UniProtKB:Q6YMS4
ChainResidueDetails
ALYS61
AASP146
ALYS182
AGLU218

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:27866982
ChainResidueDetails
ALYS13
AGLU149
AARG213

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:27866982
ChainResidueDetails
ASER56
ATHR104

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:27633330, ECO:0000269|PubMed:27866982, ECO:0000269|PubMed:28031359
ChainResidueDetails
AGLY86
ATRP87
ALYS105
AASP131
AVAL132

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:27633330, ECO:0000269|PubMed:27866982, ECO:0000269|PubMed:28031359
ChainResidueDetails
AHIS110
AGLU111
AASP146

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00924
ChainResidueDetails
AILE147
ATYR220

site_idSWS_FT_FI7
Number of Residues7
DetailsSITE: mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
ChainResidueDetails
ALYS13
AASN17
APHE24
ALYS28
ASER150
AARG213
ASER215

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: mRNA cap binding; via carbonyl oxygen => ECO:0000255|PROSITE-ProRule:PRU00924
ChainResidueDetails
ALEU16
AMET19

site_idSWS_FT_FI9
Number of Residues3
DetailsSITE: Essential for 2'-O-methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924
ChainResidueDetails
ALYS61
ALYS182
AGLU218

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Essential for 2'-O-methyltransferase and N-7 methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924
ChainResidueDetails
AASP146

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P03314
ChainResidueDetails
ASER56

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon