MolNFT v1 · #53160 · protein
Structural and thermodynamic consequences of cyclization of peptide ligands for the recruitment site of cyclin a
2WMB: “Structural and thermodynamic consequences of cyclization of peptide ligands for the recruitment site of…”. X-ray diffraction. MolNFT v1 #53160 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2WMB
- Type
- protein
- Length
- 1,085 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P24941, P20248
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 297 | — | P24941 |
| B, D | — | protein | 258 | — | P20248 |
| C | — | protein | 267 | — | P24941 |
| I | — | protein | 5 | — | — |
Compared structures
- 2WMB · Structural and thermodynamic consequences of cyclization of peptide ligands for the… · the same entry in another collection · chain I against I, 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
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
- Elsewhere: RCSB PDB 2WMB · PDBe 2WMB · UniProt P24941 · UniProt P20248
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