1O9K: Retinoblastoma tumour suppressor protein

Crystal structure of the retinoblastoma tumour suppressor protein bound to E2F peptide. Determined by X-ray diffraction at 2.6 Å resolution. Released 6 Mar 2003.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: HOMO SAPIENS
Chains: 12
Atoms: 11,974
Mol. weight: 181.97 kDa
Released: 6 Mar 2003

Explore 1O9K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1O9K contains 93 α-helices and 8 β-strands across 12 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: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	382-391	10
α-helix	398-405	8
α-helix	412-433	22
α-helix	441-468	28
α-helix	474-478	5
α-helix	480-497	18
α-helix	515-521	7
α-helix	525-538	14
α-helix	544-559	16
α-helix	561-563	3
α-helix	569-576	8

Chain B: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
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	742-743	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	780-783	4

Chain C: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	382-391	10
α-helix	398-405	8
α-helix	412-433	22
α-helix	441-465	25
α-helix	474-477	4
α-helix	480-497	18
α-helix	515-521	7
α-helix	525-529	5
α-helix	532-538	7
α-helix	544-559	16
α-helix	561-563	3
α-helix	569-576	8

Chain D: 11 helices, 2 β-strands

Element	Residues	Length	Sheet
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	2
β-strand	749-750	2	2
α-helix	752-755	4
α-helix	756-760	5
α-helix	761-768	8
α-helix	776-777	2
α-helix	781-783	3

Chain E: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	383-388	6
α-helix	398-404	7
α-helix	412-434	23
α-helix	436-438	3
α-helix	439-467	29
α-helix	474-477	4
α-helix	480-498	19
α-helix	516-521	6
α-helix	525-538	14
α-helix	544-559	16
α-helix	561-563	3
α-helix	569-576	8

Chain F: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
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	742-743	2	3
β-strand	749-750	2	3
α-helix	752-755	4
α-helix	756-760	5
α-helix	761-769	9
α-helix	780-783	4

Chain G: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	381-387	7
α-helix	398-404	7
α-helix	412-434	23
α-helix	436-438	3
α-helix	439-467	29
α-helix	474-477	4
α-helix	480-499	20
α-helix	514-520	7
α-helix	525-529	5
α-helix	532-538	7
α-helix	544-559	16
α-helix	561-563	3
α-helix	569-574	6

Chain H: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
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	742-743	2	4
β-strand	749-750	2	4
α-helix	752-755	4
α-helix	756-760	5
α-helix	761-769	9
α-helix	777-782	6

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Retinoblastoma-associated protein	A, C, E, G	protein	218	HOMO SAPIENS	P06400 (AlphaFold model)
Retinoblastoma-associated protein	B, D, F, H	protein	152	HOMO SAPIENS	P06400 (AlphaFold model)
Transcription factor E2F1	P, Q, R, S	protein	18	HOMO SAPIENS	Q01094 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>1O9K_1 RETINOBLASTOMA-ASSOCIATED PROTEIN (chains A, C, E, G)
HTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFA
KAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACAL
EVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLE
RCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHLESA

Sequence of entity 2 (B, D, F, H), FASTA

>1O9K_2 RETINOBLASTOMA-ASSOCIATED PROTEIN (chains B, D, F, H)
FQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELM
RDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVF
YNSVFMQRLKTNILQYASTRPPTLSPIPHIPR

Sequence of entity 3 (P, Q, R, S), FASTA

>1O9K_3 TRANSCRIPTION FACTOR E2F1 (chains P, Q, R, S)
LDYHFGLEEGEGIRDLFD

Primary citation

Crystal Structure of the Retinoblastoma Tumor Suppressor Protein Bound to E2F and the Molecular Basis of its Regulation. Xiao, B., Spencer, J., Clements, A. et al. Proc Natl Acad Sci U S A (2003) 100:2363. DOI 10.1073/PNAS.0436813100 · 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…

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