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3PEN

Structure of archaeal initiation factor aIF2gamma subunit delta 37-47 from Sulfolobus solfataricus in the GDP-bound form.

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
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP A 416
ChainResidue
AASP19
AASP152
ASER184
AALA185
ALEU186
AMG419
AHOH530
AHOH574
AHOH580
AHOH622
AHOH626
AHIS20
AHOH638
AHOH652
AHOH660
AGLY21
ALYS22
ATHR23
ATHR24
AHOH41
AASN149
ALYS150

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 5GP A 1
ChainResidue
APHE221
AVAL223
ALYS234
ASER278
AARG280
AGLY282
AALA296
AGLY298
AHOH661
AHOH668

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 417
ChainResidue
ATHR54
ATHR70
AHOH591
AHOH594
AHOH603
AHOH611

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 418
ChainResidue
AVAL151
AVAL154
ATRP327
AASN328
AHOH582
AHOH596

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 419
ChainResidue
ATHR23
ALYS48
AGDP416
AHOH574
AHOH589

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 420
ChainResidue
AGLU66
ATYR68
AASP192
AHOH581
AHOH617

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 421
ChainResidue
AMET111
AHOH588
AHOH601
AHOH610
AHOH615
AHOH616

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsRegion: {"description":"G1","evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsRegion: {"description":"G3","evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsRegion: {"description":"G4","evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsRegion: {"description":"G5","evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
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_FI6
Number of Residues1
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_FI7
Number of Residues1
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_FI8
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8U082","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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