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CDK2/CYCLIN a in complex with an 11-residue recruitment peptide from retinoblastoma-associated protein

Analyse CDK2/CYCLIN a in complex with an 11-residue recruitment peptide from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H25
Type: protein
Length: 1,099 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P24941, P20248, P06400

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	294	—	P24941
B, D	—	protein	258	—	P20248
C	—	protein	279	—	P24941
E	—	protein	10	—	P06400

Compared structures

1H25 · CDK2/Cyclin A in complex with an 11-residue recruitment peptide from… · the same entry in another collection · chain E against E, TM-score 1.00
P20248 · AlphaFold monomer V2.0 prediction for cyclin-A2 (P20248) · a predicted model of the same protein · chain B against A, TM-score 1.00
P24941 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase 2 (P24941) · a predicted model of the same protein · chain A against A, TM-score 0.91
P06400 · AlphaFold monomer V2.0 prediction for retinoblastoma-associated protein (P06400) · a predicted model of the same protein · chain E against A, TM-score 0.32

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P24941
Every structure of UniProt P20248
Every structure of UniProt P06400
Elsewhere: RCSB PDB 1H25 · PDBe 1H25 · UniProt P24941 · UniProt P20248 · UniProt P06400

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