4ELJ: Retinoblastoma-associated protein

Name: PDB 4ELJ: Crystal structure of the inactive retinoblastoma protein phosphorylated at T373
Published: 2012-05-23
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: cell cycle

Crystal structure of the inactive retinoblastoma protein phosphorylated at T373. Determined by X-ray diffraction at 2.7 Å resolution. Released 23 May 2012.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 1
Atoms: 4,908
Mol. weight: 76.37 kDa
Released: 23 May 2012

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

Secondary structure: helices and β-sheets

4ELJ contains 41 α-helices and 6 β-strands across 1 chain. 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: 41 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	55-63	9
α-helix	68-84	17
α-helix	96-109	14
α-helix	117-124	8
α-helix	128-137	10
α-helix	142-169	28
β-strand	173	1	1
α-helix	187-205	19
α-helix	212-229	18
α-helix	232-234	3
β-strand	235	1	1
α-helix	237-240	4
α-helix	272-280	9
α-helix	285-291	7
α-helix	292-296	5
α-helix	297-301	5
α-helix	304-306	3
β-strand	307-308	2	2
β-strand	311-312	2	2
α-helix	314-328	15
α-helix	333-338	6
α-helix	341-343	3
α-helix	374-388	15
α-helix	398-405	8
α-helix	412-434	23
α-helix	436-438	3
α-helix	439-468	30
α-helix	474-478	5
α-helix	480-498	19
α-helix	500-501	2
α-helix	516-520	5
α-helix	525-538	14
α-helix	544-559	16
α-helix	561-563	3
α-helix	569-574	6
α-helix	646-669	24
α-helix	675-690	16
α-helix	692-694	3
α-helix	700-714	15
α-helix	721-729	9
α-helix	737-740	4
β-strand	742-745	4	3
β-strand	748-750	3	3
α-helix	752-755	4
α-helix	756-760	5
α-helix	761-764	4
α-helix	768-770	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Retinoblastoma-associated protein	A	protein	656	Homo sapiens	P06400 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4ELJ_1 Retinoblastoma-associated protein (chains A)
GEFEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVD
LDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTC
ELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKL
SPPMLLKEPYKTAVIENDTRIIEVLCKEHECNIDEVANVAFKNFIPFMNSLGLVTSNGLP
EVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPH
TPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAK
AVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALE
VVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLER
CEHRIMESLAWLSDSPLFDLIKQSKDREGPLKSTSLSLFYKKVYRLAYLRLNTLCERLLS
EHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDL
PHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLAPIPHIPR

Primary citation

Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. Burke, J.R., Hura, G.L., Rubin, S.M. Genes Dev (2012) 26:1156-1166. DOI 10.1101/gad.189837.112 · PubMed

Other PDB entries of the same protein (UniProt P06400 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2R7G 1.67 Å, Structure of the retinoblastoma protein pocket domain in complex with adenovirus E1A CR1…
1GUX 1.85 Å, Rb pocket bound to E7 lxcxe motif
4ELL 1.98 Å, Structure of the inactive retinoblastoma protein pocket domain
2QDJ 2.0 Å, Crystal structure of the Retinoblastoma protein N-domain provides insight into tumor…
9DHU 2.16 Å, The Retinoblastoma Protein with Mutation E533K
1N4M 2.2 Å, Structure of Rb tumor suppressor bound to the transactivation domain of E2F-2
9DHF 2.26 Å, The Retinoblastoma Protein with Mutation E554K
1AD6 2.3 Å, Domain A of human retinoblastoma tumor suppressor
9DHC 2.32 Å, The Retinoblastoma Protein with Mutation S751Y
4CRI 2.35 Å, Crystal Structure of 53BP1 tandem tudor domains in complex with methylated K810 Rb peptide
9DGK 2.38 Å, The Retinoblastoma Protein with Mutation M704V
1H25 2.5 Å, CDK2/Cyclin A in complex with an 11-residue recruitment peptide from…

Browse structure collections

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