1N4M: Rb tumor suppressor

Structure of Rb tumor suppressor bound to the transactivation domain of E2F-2. Determined by X-ray diffraction at 2.2 Å resolution. Released 7 Jan 2003.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 5
Atoms: 6,249
Mol. weight: 86.74 kDa
Released: 7 Jan 2003

Explore 1N4M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1N4M contains 48 α-helices and 4 β-strands across 4 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	384-391	8
α-helix	396-397	2
α-helix	398-405	8
α-helix	412-434	23
α-helix	436-438	3
α-helix	439-468	30
α-helix	474-477	4
α-helix	480-497	18
α-helix	499-503	5
α-helix	515-520	6
α-helix	525-538	14
α-helix	544-559	16
α-helix	561-563	3
α-helix	569-578	10
α-helix	645-669	25
α-helix	678-690	13
α-helix	692-695	4
α-helix	700-714	15
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	761-770	10
α-helix	776-783	8

Chain B: 22 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	382-389	8
α-helix	396-397	2
α-helix	398-405	8
α-helix	412-431	20
α-helix	439-468	30
α-helix	474-477	4
α-helix	480-497	18
α-helix	514-520	7
α-helix	525-536	12
α-helix	544-559	16
α-helix	561-563	3
α-helix	569-576	8
α-helix	645-669	25
α-helix	674-690	17
α-helix	692-695	4
α-helix	700-713	14
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	776-783	8

Chains C and D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	422-424	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Retinoblastoma Pocket	A, B	protein	345	Homo sapiens	P06400 (AlphaFold model)
Transcription factor E2F2	C, D, E	protein	18		Q14209 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1N4M_1 Retinoblastoma Pocket (chains A, B)
NTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGAGCV
AIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYS
RSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIME
SLAWLSDSPLFDLIKQSKTREGKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHII
WTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFK
RVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHI

Sequence of entity 2 (C, D, E), FASTA

>1N4M_2 Transcription factor E2F2 (chains C, D, E)
DDYLWGLEAGEGISDLFD

Primary citation

Structural basis for the recognition of the E2F transactivation domain by the retinoblastoma tumor suppressor. Lee, C., Chang, J.H., Lee, H.S. et al. Genes Dev (2002) 16:3199-3212. DOI 10.1101/gad.1046102 · 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
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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