2R7G: Retinoblastoma protein pocket domain

Structure of the retinoblastoma protein pocket domain in complex with adenovirus E1A CR1 domain. Determined by X-ray diffraction at 1.67 Å resolution. Released 2 Oct 2007.

Method: X-ray diffraction
Resolution: 1.67 Å
Organisms: Homo sapiens, Human adenovirus 5
Chains: 5
Atoms: 6,267
Mol. weight: 85.24 kDa
Released: 2 Oct 2007

Explore 2R7G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2R7G contains 47 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: 22 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	382-391	10
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	480-501	22
α-helix	516-521	6
α-helix	525-538	14
α-helix	544-559	16
α-helix	561-563	3
α-helix	569-577	9
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	776-784	9

Chains B and D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	43-46	4

Chain C: 23 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	382-391	10
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	480-501	22
α-helix	516-521	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	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	2
β-strand	749-750	2	2
α-helix	752-755	4
α-helix	756-760	5
α-helix	761-769	9
α-helix	770-772	3
α-helix	776-784	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Retinoblastoma-associated protein	A, C	protein	347	Homo sapiens	P06400 (AlphaFold model)
Early E1A 32 kDa protein	B, D, E	protein	10	Human adenovirus 5	P03255 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>2R7G_1 Retinoblastoma-associated protein (chains A, C)
NTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCV
EIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYS
RSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIME
SLAWLSDSPLFDLIKQSKDREGKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHII
WTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFK
RVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPR

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

>2R7G_2 Early E1A 32 kDa protein (chains B, D, E)
PPTLHELYDL

Primary citation

Structure of the retinoblastoma protein bound to adenovirus E1A reveals the molecular basis for viral oncoprotein inactivation of a tumor suppressor. Liu, X., Marmorstein, R. Genes Dev (2007) 21:2711-2716. DOI 10.1101/gad.1590607 · PubMed

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

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

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