4C9B: EIF4AIII-CWC22 complex

Crystal structure of eIF4AIII-CWC22 complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 13 Nov 2013.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
5,695
Mol. weight
81.36 kDa
Ligands
PO4
Released
13 Nov 2013

Explore 4C9B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4C9B contains 42 α-helices and 21 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: 26 helices, 18 β-strands

ElementResiduesLengthSheet
α-helix23-253
β-strand28-3031
α-helix40-423
α-helix47-5610
α-helix61-622
α-helix65-739
β-strand78-8141
α-helix88-9811
β-strand109-11241
α-helix116-12914
β-strand137-13931
α-helix143-1453
α-helix146-15510
β-strand159-16241
α-helix164-17310
β-strand183-18641
α-helix189-1957
α-helix198-2069
β-strand213-21861
α-helix223-23210
α-helix2361
β-strand237-24151
α-helix242-2432
β-strand246-24722
β-strand251-25993
α-helix261-2633
α-helix264-27411
β-strand279-28353
α-helix287-29913
β-strand304-30743
α-helix313-32513
β-strand330-33343
β-strand346-35163
α-helix360-3656
α-helix3661
β-strand367-36822
α-helix372-3743
β-strand375-38283
α-helix383-3853
α-helix386-39611
β-strand401-40223
α-helix4031
β-strand40414
α-helix405-4106
Chain B: 16 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix127-1282
β-strand13214
α-helix136-1405
α-helix150-17223
α-helix178-1869
α-helix194-20714
α-helix209-2113
α-helix212-22514
α-helix227-24721
α-helix250-26516
β-strand26915
α-helix272-28312
α-helix287-30721
α-helix309-32416
α-helix330-34415
α-helix362-3643
β-strand36815
α-helix380-3834
α-helix391-40515

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Eukaryotic initiation factor 4A-IIIAprotein411HOMO SAPIENSP38919 (AlphaFold model)
Pre-mRNA-splicing factor CWC22 homologBprotein291HOMO SAPIENSQ9HCG8 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4C9B_1 EUKARYOTIC INITIATION FACTOR 4A-III (chains A)
MATTATMATSGSARKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEK
PSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILAPTRELAV
QIQKGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRA
IKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRIL
VKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREA
NFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNREL
YIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI
Sequence of entity 2 (B), FASTA
>4C9B_2 PRE-MRNA-SPLICING FACTOR CWC22 HOMOLOG (chains B)
KKKKDELDPLLTRTGGAYIPPAKLRMMQEQITDKNSLAYQRMSWEALKKSINGLINKVNI
SNISIIIQELLQENIVRGRGLLSRSVLQAQSASPIFTHVYAALVAIINSKFPQIGELILK
RLILNFRKGYRRNDKQLCLTASKFVAHLINQNVAHEVLCLEMLTLLLERPTDDSVEVAIG
FLKECGLKLTQVSPRGINAIFERLRNILHESEIDKRVQYMIEVMFAVRKDGFKDHPIILE
GLDLVEEDDQFTHMLPLEDDYNPEDVLNVFKMDPNFMENEEKYKAIKKEIL

Ligands and cofactors

IDNameFormulaCopies
PO4Phosphate ionO4 P1

Water and common crystallization additives (GOL) are not listed.

Primary citation

Crystal Structure of the Human Eif4Aiii-Cwc22 Complex Shows How a Dead-Box Protein is Inhibited by a Mif4G Domain. Buchwald, G., Schuessler, S., Basquin, C. et al. Proc Natl Acad Sci U S A (2013) 110:E4611. DOI 10.1073/PNAS.1314684110 · PubMed

Other PDB entries of the same protein (UniProt P38919 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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