3EIJ: Pdcd4

Crystal structure of Pdcd4. Determined by X-ray diffraction at 2.8 Å resolution. Released 17 Feb 2009.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,418
Mol. weight: 71.52 kDa
Released: 17 Feb 2009

Explore 3EIJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3EIJ contains 35 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: 17 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	158-178	21
α-helix	181-190	10
α-helix	195-198	4
α-helix	199-209	11
α-helix	214-226	13
β-strand	227	1	1
β-strand	231	1	1
α-helix	233-245	13
α-helix	247-253	7
α-helix	257-270	14
α-helix	289-305	17
α-helix	326-341	16
α-helix	344-353	10
α-helix	357-359	3
α-helix	361-373	13
α-helix	377-392	16
α-helix	398-418	21
α-helix	422-435	14
α-helix	441-446	6

Chain B: 18 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	158-178	21
α-helix	181-191	11
α-helix	195-198	4
α-helix	199-209	11
α-helix	214-226	13
β-strand	227	1	2
β-strand	231	1	2
α-helix	233-245	13
α-helix	247-253	7
α-helix	257-270	14
α-helix	276-278	3
α-helix	289-305	17
α-helix	326-341	16
α-helix	344-353	10
α-helix	357-359	3
α-helix	360-373	14
α-helix	379-392	14
α-helix	398-418	21
α-helix	422-435	14
α-helix	441-445	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Programmed cell death protein 4	A, B	protein	321	Homo sapiens	Q53EL6 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3EIJ_1 Programmed cell death protein 4 (chains A, B)
GPLGSPEFLPLDERAFEKTLTPIIQEYFEHGDTNEVAEMLRDLNLGEMKSGVPVLAVSLA
LEGKASHREMTSKLLSDLCGTVMSTTDVEKSFDKLLKDLPELALDTPRAPQLVGQFIARA
VGDGILCNTYIDSYKGTVDCVQARAALDKATVLLSMSKGGKRKDSVWGSGGGQQSVNHLV
KEIDMLLKEYLLSGDISEAEHCLKELEVPHFHHELVYEAIIMVLESTGESTFKMILDLLK
SLWKSSTITVDQMKRGYERIYNEIPDINLDVPHSYSVLERFVEECFQAGIISKQLRDLCP
SRGRKRFVSEGDGGRLKPESY

Primary citation

Structural basis for translational inhibition by the tumour suppressor Pdcd4. Loh, P.G., Yang, H.-S., Walsh, M.A. et al. EMBO J (2009) 28:274-285. DOI 10.1038/emboj.2008.278 · PubMed

Other PDB entries of the same protein (UniProt Q53EL6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9TES 1.22 Å, Crystal structure of beta-TrCP bound by diphosphorylated PDCD4 degron peptide
2RG8 1.8 Å, Crystal Structure of Programmed for Cell Death 4 Middle MA3 domain
9BKD 2.6 Å, The structure of human Pdcd4 bound to the 40S small ribosomal subunit
2ZU6 2.8 Å, crystal structure of the eIF4A-PDCD4 complex
8XXL 2.9 Å, Cryo-EM structure of the human 40S ribosome with PDCD4
8XXM 3.2 Å, Cryo-EM structure of the human 40S ribosome with PDCD4 and eIF3G
8XXN 3.6 Å, Cryo-EM structure of the human 43S ribosome with PDCD4
9BLN 3.9 Å, The structure of human Pdcd4 bound to the 40S-eIF4A-eIF3-eIF1 complex
2GGF Solution structure of the MA3 domain of human Programmed cell death 4
2KZT Structure of the Tandem MA-3 Region of Pdcd4

Browse structure collections

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