Research workbench
Solution structure of the BEM1P SH3-ci domain from L.ELONGISPORUS in complex with STE20P peptide
Analyse Solution structure of the BEM1P SH3-ci domain from L.ELONGISPORUS in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KYM
- Type
- protein
- Length
- 136 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A5E3P5, Q03497
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 120 | — | A5E3P5 |
| B | — | protein | 16 | — | Q03497 |
Compared structures
- 2KYM · Solution structure of the Bem1p SH3-CI domain from L.elongisporus in complex with Ste20p… · the same entry in another collection · chain A against A, TM-score 1.00
- Q03497 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase STE20 (Q03497) · a predicted model of the same protein · chain B against A, TM-score 0.24
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 A5E3P5
- Every structure of UniProt Q03497
- Elsewhere: RCSB PDB 2KYM · PDBe 2KYM · UniProt A5E3P5 · UniProt Q03497
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.