1UG3: C-terminal portion of human eIF4GI

C-terminal portion of human eIF4GI. Determined by X-ray diffraction at 2.24 Å resolution. Released 22 Mar 2005.

Method: X-ray diffraction
Resolution: 2.24 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,370
Mol. weight: 76.58 kDa
Released: 22 Mar 2005

Explore 1UG3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1UG3 contains 47 α-helices and 4 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 24 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	1235-1257	23
α-helix	1260-1268	9
α-helix	1273-1275	3
α-helix	1276-1287	12
α-helix	1292-1307	16
α-helix	1313-1330	18
α-helix	1337-1345	9
α-helix	1346-1349	4
α-helix	1356-1363	8
α-helix	1367-1370	4
α-helix	1373-1388	16
α-helix	1390-1399	10
α-helix	1404-1406	3
α-helix	1409	1
α-helix	1414-1420	7
α-helix	1424-1426	3
α-helix	1440-1453	14
α-helix	1458-1468	11
α-helix	1471-1474	4
α-helix	1477-1490	14
β-strand	1492-1493	2	1
β-strand	1499-1500	2	1
α-helix	1502-1515	14
α-helix	1519-1535	17
α-helix	1542-1552	11
α-helix	1558-1564	7

Chain B: 23 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	1235-1257	23
α-helix	1260-1268	9
α-helix	1273-1275	3
α-helix	1276-1287	12
α-helix	1292-1307	16
α-helix	1313-1330	18
α-helix	1337-1345	9
α-helix	1346-1349	4
α-helix	1356-1363	8
α-helix	1367-1370	4
α-helix	1373-1388	16
α-helix	1390-1399	10
α-helix	1404-1406	3
α-helix	1414-1420	7
α-helix	1424-1426	3
α-helix	1440-1453	14
α-helix	1458-1468	11
α-helix	1471-1474	4
α-helix	1477-1490	14
β-strand	1492-1493	2	2
β-strand	1499-1500	2	2
α-helix	1502-1515	14
α-helix	1519-1535	17
α-helix	1542-1552	11
α-helix	1558-1564	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
eukaryotic protein synthesis initiation factor 4G	A, B	protein	339	Homo sapiens	Q04637 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1UG3_1 eukaryotic protein synthesis initiation factor 4G (chains A, B)
SKAALSEEELEKKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRHGVESTLERSAI
AREHMGQLLHQLLCAGHLSTAQYYQGLYEILELAEDMEIDIPHVWLYLAELVTPILQEGG
VPMGELFREITKPLRPLGKAASLLLEILGLLCKSMGPKKVGTLWREAGLSWKEFLPEGQD
IGAFVAEQKVEYTLGEESEAPGQRALPSEELNRQLEKLLKEGSSNQRVFDWIEANLSEQQ
IVSNTLVRALMTAVCYSAIIFETPLRVDVAVLKARAKLLQKYLCDEQKELQALYALQALV
VTLEQPPNLLRMFFDALYDEDVVKEDAFYSWESSKDPAE

Primary citation

Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1. Bellsolell, L., Cho-Park, P.F., Poulin, F. et al. Structure (2006) 14:913-923. DOI 10.1016/j.str.2006.03.012 · PubMed

Other PDB entries of the same protein (UniProt Q04637 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5T46 1.53 Å, Crystal structure of the human eIF4E-eIF4G complex
5EI3 1.71 Å, Co-crystal structure of eIF4E with nucleotide mimetic inhibitor.
4F02 2.0 Å, Crystal structure of the PABP-binding site of eIF4G in complex with RRM1-2 of PABP and…
4AZA 2.16 Å, Improved eIF4E binding peptides by phage display guided design.
5ZK5 2.25 Å, Stapled-peptides tailored against initiation of translation
2W97 2.29 Å, Crystal Structure of eIF4E Bound to Glycerol and eIF4G1 peptide
1LJ2 2.38 Å, Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization
5EHC 2.4 Å, Co-crystal structure of eIF4E with nucleotide mimetic inhibitor.
5EIR 2.69 Å, Co-crystal structure of eIF4E with nucleotide mimetic inhibitor.
8OZ0 3.5 Å, Structure of a human 48S translation initiation complex with eIF4F and eIF4A
6ZMW 3.7 Å, Structure of a human 48S translational initiation complex
8J7R 3.7 Å, Cryo-EM structure of the J-K-St region of EMCV IRES in complex with eIF4G-HEAT1 and…

Browse structure collections

About this viewer

MolViewer shows 1UG3 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.