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6H6K

The structure of the FKR mutant of the archaeal translation initiation factor 2 gamma subunit in complex with GDPCP, obtained in the absence of magnesium salts in the crystallization solution.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0001731biological_processformation of translation preinitiation complex
A0003743molecular_functiontranslation initiation factor activity
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0006412biological_processtranslation
A0006413biological_processtranslational initiation
A0006414biological_processtranslational elongation
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0000049molecular_functiontRNA binding
B0000166molecular_functionnucleotide binding
B0001731biological_processformation of translation preinitiation complex
B0003743molecular_functiontranslation initiation factor activity
B0003746molecular_functiontranslation elongation factor activity
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0006412biological_processtranslation
B0006413biological_processtranslational initiation
B0006414biological_processtranslational elongation
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0000049molecular_functiontRNA binding
C0000166molecular_functionnucleotide binding
C0001731biological_processformation of translation preinitiation complex
C0003743molecular_functiontranslation initiation factor activity
C0003746molecular_functiontranslation elongation factor activity
C0003924molecular_functionGTPase activity
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0006412biological_processtranslation
C0006413biological_processtranslational initiation
C0006414biological_processtranslational elongation
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0000049molecular_functiontRNA binding
D0000166molecular_functionnucleotide binding
D0001731biological_processformation of translation preinitiation complex
D0003743molecular_functiontranslation initiation factor activity
D0003746molecular_functiontranslation elongation factor activity
D0003924molecular_functionGTPase activity
D0005515molecular_functionprotein binding
D0005525molecular_functionGTP binding
D0006412biological_processtranslation
D0006413biological_processtranslational initiation
D0006414biological_processtranslational elongation
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
E0000049molecular_functiontRNA binding
E0000166molecular_functionnucleotide binding
E0001731biological_processformation of translation preinitiation complex
E0003743molecular_functiontranslation initiation factor activity
E0003746molecular_functiontranslation elongation factor activity
E0003924molecular_functionGTPase activity
E0005515molecular_functionprotein binding
E0005525molecular_functionGTP binding
E0006412biological_processtranslation
E0006413biological_processtranslational initiation
E0006414biological_processtranslational elongation
E0016787molecular_functionhydrolase activity
E0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
Detailsbinding site for residue GCP A 501
ChainResidue
AVAL18
ALYS150
AASP152
AVAL153
ASER184
AALA185
ALEU186
AHOH604
AHOH606
AHOH614
AHOH654
AASP19
AHOH718
AHOH724
AHOH744
AHOH749
AHOH774
AHIS20
AGLY21
ALYS22
ATHR23
ATHR24
AGLY96
AASN149

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 502
ChainResidue
AMET111
AHOH675
AHOH678
AHOH777
AHOH808
AHOH842

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 503
ChainResidue
ATHR54
ATHR70
AHOH662
AHOH670
AHOH776
AHOH815

site_idAC4
Number of Residues6
Detailsbinding site for residue NA A 504
ChainResidue
AVAL151
AVAL154
CTRP327
CASN328
CHOH708
CHOH727

site_idAC5
Number of Residues21
Detailsbinding site for residue GCP B 501
ChainResidue
BVAL18
BASP19
BHIS20
BGLY21
BLYS22
BTHR23
BTHR24
BGLY96
BASN149
BLYS150
BASP152
BVAL153
BSER184
BALA185
BLEU186
BHOH601
BHOH606
BHOH627
BHOH712
BHOH733
BHOH753

site_idAC6
Number of Residues6
Detailsbinding site for residue NA B 502
ChainResidue
BVAL151
BVAL154
DTRP327
DASN328
DHOH717
DHOH720

site_idAC7
Number of Residues6
Detailsbinding site for residue NA B 503
ChainResidue
BTHR54
BTHR70
BHOH649
BHOH693
BHOH727
BHOH776

site_idAC8
Number of Residues5
Detailsbinding site for residue NA B 504
ChainResidue
BGLU66
BTYR68
BASP192
BHOH625
BHOH769

site_idAC9
Number of Residues17
Detailsbinding site for residue GCP C 501
ChainResidue
CVAL18
CASP19
CHIS20
CGLY21
CLYS22
CTHR23
CTHR24
CTHR46
CGLY96
CASN149
CLYS150
CASP152
CVAL153
CSER184
CALA185
CLEU186
CHOH681

site_idAD1
Number of Residues7
Detailsbinding site for residue EDO C 502
ChainResidue
CSER364
CVAL386
CALA387
CHOH615
CHOH623
CSER314
CVAL361

site_idAD2
Number of Residues3
Detailsbinding site for residue EDO C 503
ChainResidue
CLEU305
CHOH627
DLEU305

site_idAD3
Number of Residues4
Detailsbinding site for residue EDO C 504
ChainResidue
CLYS254
CALA319
DLYS275
DTYR300

site_idAD4
Number of Residues15
Detailsbinding site for residue GCP D 501
ChainResidue
DVAL18
DASP19
DHIS20
DGLY21
DLYS22
DTHR23
DTHR24
DGLY96
DASN149
DLYS150
DASP152
DSER184
DALA185
DLEU186
DHOH648

site_idAD5
Number of Residues8
Detailsbinding site for residue EDO D 502
ChainResidue
DSER314
DVAL361
DSER364
DVAL386
DALA387
DTRP389
DHOH616
DHOH623

site_idAD6
Number of Residues19
Detailsbinding site for residue GCP E 501
ChainResidue
EVAL18
EASP19
EHIS20
EGLY21
ELYS22
ETHR23
ETHR24
EMET45
ETHR46
EGLY96
EASN149
ELYS150
EASP152
EVAL153
ESER184
EALA185
ELEU186
EHOH602
EHOH632

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues35
DetailsRegion: {"description":"G1","evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsRegion: {"description":"G2","evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues15
DetailsRegion: {"description":"G3","evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues15
DetailsRegion: {"description":"G4","evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsRegion: {"description":"G5","evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues50
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25690901","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RCY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RD1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25690901","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RD1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16407071","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25690901","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AHO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8U082","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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