4ELL: Inactive retinoblastoma protein pocket domain

Name: PDB 4ELL: Structure of the inactive retinoblastoma protein pocket domain
Published: 2012-05-23
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: cell cycle

Structure of the inactive retinoblastoma protein pocket domain. Determined by X-ray diffraction at 1.98 Å resolution. Released 23 May 2012.

Method: X-ray diffraction
Resolution: 1.98 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,961
Mol. weight: 95.35 kDa
Released: 23 May 2012

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

Secondary structure: helices and β-sheets

4ELL contains 48 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: 23 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	384-391	8
α-helix	398-405	8
α-helix	412-434	23
α-helix	441-467	27
α-helix	470-477	8
α-helix	480-497	18
α-helix	516-520	5
α-helix	525-538	14
α-helix	544-559	16
α-helix	561-563	3
α-helix	568-575	8
α-helix	602-607	6
α-helix	645-669	25
α-helix	676-690	15
α-helix	692-695	4
α-helix	700-713	14
α-helix	721-728	8
α-helix	737-740	4
β-strand	742-743	2	1
β-strand	749-750	2	1
α-helix	752-755	4
α-helix	756-760	5
α-helix	761-769	9
α-helix	770-772	3
α-helix	776-782	7

Chain B: 25 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	385-391	7
α-helix	398-405	8
α-helix	412-434	23
α-helix	436-438	3
α-helix	439-464	26
α-helix	470-477	8
α-helix	480-497	18
α-helix	516-520	5
α-helix	525-529	5
α-helix	532-538	7
α-helix	544-559	16
α-helix	561-563	3
α-helix	568-579	12
α-helix	582-586	5
α-helix	602-607	6
α-helix	645-669	25
α-helix	676-690	15
α-helix	692-695	4
α-helix	700-714	15
α-helix	721-728	8
α-helix	737-740	4
β-strand	742-745	4	2
β-strand	748-750	3	2
α-helix	752-755	4
α-helix	756-760	5
α-helix	761-770	10
α-helix	776-785	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Retinoblastoma-associated protein	A, B	protein	411	Homo sapiens	P06400 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4ELL_1 Retinoblastoma-associated protein (chains A, B)
GEFNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQ
GCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMA
TYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHR
IMESFAWLSDSPLFDLIKQSKDREGPTDHLESACPLNLPLQNNHTAADMYLEPVRAPKKK
GSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPEL
EHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQ
ETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLAPIPHIPR

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
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…
1PJM 2.5 Å, Mouse Importin alpha-bipartite NLS from human retinoblastoma protein Complex

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