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6R8S

Crystal structure of aIF2gamma subunit I181K from archaeon Sulfolobus solfataricus complexed with GDPCP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA 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 Residues27
Detailsbinding site for residue GCP A 501
ChainResidue
AVAL18
AGLY96
AASN149
ALYS150
AASP152
ASER184
AALA185
ALEU186
AMG502
AFMT508
AHOH607
AASP19
AHOH664
AHOH672
AHOH673
AHOH676
AHOH681
AHOH703
AHOH733
AHOH749
AHIS20
AGLY21
ALYS22
ATHR23
ATHR24
AMET45
ATHR46

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 502
ChainResidue
ATHR23
ATHR46
AGCP501
AHOH673
AHOH681

site_idAC3
Number of Residues3
Detailsbinding site for residue FMT A 503
ChainResidue
AARG130
AHOH690
AHOH821

site_idAC4
Number of Residues4
Detailsbinding site for residue FMT A 504
ChainResidue
ALEU312
ASER364
ATHR365
AHOH634

site_idAC5
Number of Residues5
Detailsbinding site for residue FMT A 505
ChainResidue
AGLN251
AGLU252
AGLU344
AMET345
AHOH637

site_idAC6
Number of Residues5
Detailsbinding site for residue FMT A 506
ChainResidue
AILE32
AALA52
AGLU53
AHOH700
AHOH807

site_idAC7
Number of Residues5
Detailsbinding site for residue FMT A 507
ChainResidue
AHIS37
AARG219
AASP309
AHOH619
AHOH633

site_idAC8
Number of Residues9
Detailsbinding site for residue FMT A 508
ChainResidue
AASP152
AVAL153
AHIS187
APRO324
ALEU326
AGCP501
AHOH699
AHOH733
AHOH738

site_idAC9
Number of Residues3
Detailsbinding site for residue FMT A 509
ChainResidue
AARG43
AMET45
AHOH846

site_idAD1
Number of Residues4
Detailsbinding site for residue FMT A 510
ChainResidue
ATHR366
ALEU367
AARG383
AARG384

site_idAD2
Number of Residues3
Detailsbinding site for residue FMT A 511
ChainResidue
ATHR365
AHOH689
AHOH828

site_idAD3
Number of Residues3
Detailsbinding site for residue FMT A 513
ChainResidue
APRO125
AGLU252
AHOH773

site_idAD4
Number of Residues8
Detailsbinding site for residue FMT A 514
ChainResidue
ATRP33
ASER35
AGLU40
AGLY44
AMET45
ATHR46
AHOH673
AHOH884

site_idAD5
Number of Residues7
Detailsbinding site for residue FMT A 515
ChainResidue
ATYR206
AARG207
AASP208
AGLN211
AILE243
AHOH635
AHOH662

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00119, ECO:0000269|PubMed:25690901, ECO:0007744|PDB:4RD1
ChainResidueDetails
AASP19
AGLY44

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00119, ECO:0000269|PubMed:16407071, ECO:0000269|PubMed:25690901, ECO:0007744|PDB:2AHO
ChainResidueDetails
ATHR23
ATHR46

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8U082, ECO:0000255|HAMAP-Rule:MF_00119
ChainResidueDetails
ACYS59
ACYS62
ACYS74
ACYS77

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00119, ECO:0000269|PubMed:25690901, ECO:0007744|PDB:4RCY, ECO:0007744|PDB:4RD1
ChainResidueDetails
AASN149
ASER184

222036

PDB entries from 2024-07-03

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