Research workbench
Two binding orientations for peptides to src SH3 domain: development of a general model for SH3-ligand interactions
Analyse Two binding orientations for peptides to src SH3 domain: development of a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PRM
- Type
- protein
- Length
- 65 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-src tyrosine kinase SH3 domain; Proline-rich ligand PLR1 (afapplprr)
- UniProt
- P00523
Structure
solution nmr · 2 distinct chains · 0% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | C-src tyrosine kinase SH3 domain | protein | 56 | 0% helix, 43% strand | P00523 |
| A | Proline-rich ligand PLR1 (afapplprr) | protein | 9 | 0% helix, 0% strand | — |
Interfaces
1 interface between chains.
- C–A · 409 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1PRM · Two binding orientations for peptides to src SH3 domain: development of a general model… · the same entry in another collection · chain C against C, TM-score 1.00
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 P00523
- Elsewhere: RCSB PDB 1PRM · PDBe 1PRM · UniProt P00523
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