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3LKZ

Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003968molecular_functionRNA-dependent RNA polymerase activity
A0004482molecular_functionmRNA 5'-cap (guanine-N7-)-methyltransferase activity
A0004483molecular_functionmRNA (nucleoside-2'-O-)-methyltransferase activity
A0005524molecular_functionATP binding
A0008168molecular_functionmethyltransferase activity
A0032259biological_processmethylation
B0003968molecular_functionRNA-dependent RNA polymerase activity
B0004482molecular_functionmRNA 5'-cap (guanine-N7-)-methyltransferase activity
B0004483molecular_functionmRNA (nucleoside-2'-O-)-methyltransferase activity
B0005524molecular_functionATP binding
B0008168molecular_functionmethyltransferase activity
B0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SFG A 301
ChainResidue
ASER56
AGLU111
AVAL130
AASP131
AVAL132
APHE133
AASP146
AILE147
AGLU149
AHOH376
AHOH396
AGLY58
AHOH425
BARG200
AGLY81
ACYS82
AGLY83
AGLY86
ATRP87
ALYS105
AHIS110

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
AHIS159
ALYS246
AARG247
ATHR248
AHOH463
AHOH496
BARG177

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SFG B 301
ChainResidue
AARG200
BSER56
BGLY58
BGLY81
BCYS82
BGLY83
BGLY86
BTRP87
BTHR104
BLYS105
BHIS110
BGLU111
BVAL130
BASP131
BVAL132
BPHE133
BASP146
BGLU149
BHOH386
BHOH397
BHOH512

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
AARG177
BHIS159
BLYS246
BARG247
BTHR248
BHOH483

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: For 2'-O-MTase activity => ECO:0000269|PubMed:17267492
ChainResidueDetails
ALYS61
AASP146
ALYS182
AGLU218
BLYS61
BASP146
BLYS182
BGLU218

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:17267492
ChainResidueDetails
ASER56
BSER56

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0007744|PDB:2OY0
ChainResidueDetails
AGLY86
ATRP87
AASP131
AVAL132
BGLY86
BTRP87
BASP131
BVAL132

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00924
ChainResidueDetails
ATHR104
ALYS105
AILE147
ATYR220
BTHR104
BLYS105
BILE147
BTYR220

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17267492
ChainResidueDetails
AGLU111
AASP146
BGLU111
BASP146

site_idSWS_FT_FI6
Number of Residues12
DetailsSITE: mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
ChainResidueDetails
ALYS13
BSER150
BARG213
BSER215
AASN17
AARG28
ASER150
AARG213
ASER215
BLYS13
BASN17
BARG28

site_idSWS_FT_FI7
Number of Residues4
DetailsSITE: mRNA cap binding; via carbonyl oxygen => ECO:0000255|PROSITE-ProRule:PRU00924
ChainResidueDetails
ALEU16
AMET19
BLEU16
BMET19

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:17267492
ChainResidueDetails
APHE24
BPHE24

site_idSWS_FT_FI9
Number of Residues6
DetailsSITE: Essential for 2'-O-methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924
ChainResidueDetails
ALYS61
ALYS182
AGLU218
BLYS61
BLYS182
BGLU218

site_idSWS_FT_FI10
Number of Residues2
DetailsSITE: Essential for 2'-O-methyltransferase and N-7 methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924
ChainResidueDetails
AASP146
BASP146

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P03314
ChainResidueDetails
ASER56
BSER56

218853

PDB entries from 2024-04-24

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