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3PEW

S. cerevisiae Dbp5 L327V bound to RNA and ADP BeF3

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003724molecular_functionRNA helicase activity
A0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ADP A 1000
ChainResidue
APHE112
AARG429
APHE430
AMG1001
ABEF1002
AHOH1010
AHOH1013
AHOH1033
AHOH1053
AHOH1087
AHOH1101
ALYS114
AHOH1107
AHOH1108
AHOH1322
AGLN119
AGLY141
ATHR142
AGLY143
ALYS144
ATHR145
AASP395

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1001
ChainResidue
AADP1000
ABEF1002
AHOH1010
AHOH1017
AHOH1096
AHOH1107

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BEF A 1002
ChainResidue
ASER140
ALYS144
AGLU240
AGLY393
AARG426
AARG429
AADP1000
AMG1001
AHOH1011
AHOH1017
AHOH1062
AHOH1096
AHOH1107

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1003
ChainResidue
AHOH1184
AHOH1204
AHOH1279
AHOH1350
AHOH1357
AHOH1448

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MG A 1004
ChainResidue
AASP264
AHOH1161
AHOH1162
AHOH1163
AHOH1164
AHOH1165
AHOH1166
AHOH1167
AHOH1453
AHOH1478

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 1005
ChainResidue
ALYS105
APHE188
AILE255
ALYS258
AARG259
AILE285

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 1006
ChainResidue
ALYS117
AILE118
ASER138
AGLN139
ATHR142
AHOH1171
AHOH1355
AHOH1463

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 1007
ChainResidue
AARG132
AASN288
AARG463
APRO465
AHOH1058
AHOH1177
AHOH1428
AHOH1455

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 1008
ChainResidue
AASN208
AARG224
AARG256
APHE260
AHOH1296

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 B 1009
ChainResidue
AGLN253
BU4
BU5

Functional Information from PROSITE/UniProt
site_idPS00039
Number of Residues9
DetailsDEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VLDEADNmL
ChainResidueDetails
AVAL237-LEU245

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
ChainResidueDetails
ASER138

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER93

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER162

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PDB entries from 2024-04-24

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