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1RZ4

Crystal Structure of Human eIF3k

Functional Information from GO Data
ChainGOidnamespacecontents
A0001732biological_processformation of cytoplasmic translation initiation complex
A0002183biological_processcytoplasmic translational initiation
A0003723molecular_functionRNA binding
A0003743molecular_functiontranslation initiation factor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005852cellular_componenteukaryotic translation initiation factor 3 complex
A0006412biological_processtranslation
A0006413biological_processtranslational initiation
A0006446biological_processregulation of translational initiation
A0016020cellular_componentmembrane
A0016282cellular_componenteukaryotic 43S preinitiation complex
A0032991cellular_componentprotein-containing complex
A0033290cellular_componenteukaryotic 48S preinitiation complex
A0043022molecular_functionribosome binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1001
ChainResidue
AARG97
AGLN101
AILE131
ATHR132
AGLY133
AHOH1037
AHOH1109

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000255|HAMAP-Rule:MF_03010, ECO:0000269|PubMed:17322308, ECO:0000269|Ref.11, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR28

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER217

218853

PDB entries from 2024-04-24

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