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6VPR

Crystal structure of the C-terminal domain of DENR

Functional Information from GO Data
ChainGOidnamespacecontents
A0001731biological_processformation of translation preinitiation complex
A0002188biological_processtranslation reinitiation
A0003674molecular_functionmolecular_function
A0003729molecular_functionmRNA binding
A0003743molecular_functiontranslation initiation factor activity
A0005515molecular_functionprotein binding
A0005575cellular_componentcellular_component
A0006412biological_processtranslation
A0006413biological_processtranslational initiation
A0032790biological_processribosome disassembly
A0075522biological_processIRES-dependent viral translational initiation
B0001731biological_processformation of translation preinitiation complex
B0002188biological_processtranslation reinitiation
B0003674molecular_functionmolecular_function
B0003729molecular_functionmRNA binding
B0003743molecular_functiontranslation initiation factor activity
B0005515molecular_functionprotein binding
B0005575cellular_componentcellular_component
B0006412biological_processtranslation
B0006413biological_processtranslational initiation
B0032790biological_processribosome disassembly
B0075522biological_processIRES-dependent viral translational initiation
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue TLA A 201
ChainResidue
AARG122
ALYS124
ALYS126
AGLN167
AHG207
BTLA301

site_idAC2
Number of Residues4
Detailsbinding site for residue TLA A 202
ChainResidue
BGLU161
ALYS142
AARG146
BGLY160

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 203
ChainResidue
ALYS126
ALYS126
ATYR127
AGLY168
AASP169

site_idAC4
Number of Residues2
Detailsbinding site for residue SO4 A 204
ChainResidue
AGLU161
BARG122

site_idAC5
Number of Residues1
Detailsbinding site for residue ACT A 205
ChainResidue
AHG207

site_idAC6
Number of Residues2
Detailsbinding site for residue HG A 206
ChainResidue
ACYS132
AGLU163

site_idAC7
Number of Residues4
Detailsbinding site for residue HG A 207
ChainResidue
ACYS154
AGLN167
ATLA201
AACT205

site_idAC8
Number of Residues6
Detailsbinding site for residue TLA B 301
ChainResidue
AGLN167
ATLA201
BARG130
BLEU193
BGLU195
BHOH401

site_idAC9
Number of Residues5
Detailsbinding site for residue TLA B 302
ChainResidue
AARG122
AALA123
ALYS125
BLYS125
BTYR127

site_idAD1
Number of Residues2
Detailsbinding site for residue PO4 B 303
ChainResidue
BGLN145
BARG146

site_idAD2
Number of Residues1
Detailsbinding site for residue SO4 B 304
ChainResidue
BASP169

site_idAD3
Number of Residues3
Detailsbinding site for residue ACT B 305
ChainResidue
BGLY155
BHG308
BHOH407

site_idAD4
Number of Residues2
Detailsbinding site for residue ACT B 306
ChainResidue
BHG307
BHOH401

site_idAD5
Number of Residues3
Detailsbinding site for residue HG B 307
ChainResidue
BCYS132
BGLU163
BACT306

site_idAD6
Number of Residues3
Detailsbinding site for residue HG B 308
ChainResidue
BCYS154
BGLN167
BACT305

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER20
BSER20

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER73
BSER73

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR86
BTHR86

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9CQJ6
ChainResidueDetails
ASER189
BSER189

218853

PDB entries from 2024-04-24

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