Research workbench
Structure of the triple (LYS(BETA)D3ALA, ASP(BETA)C8ALA, ASPCD2ALA) mutant of the src SH2 domain bound to the pqpyeeipi peptide
Analyse Structure of the triple (LYS(BETA)D3ALA, ASP(BETA)C8ALA, ASPCD2ALA) mutant of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KC2
- Type
- protein
- Length
- 104 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Src tyrosine kinase; Pqpyeeipi peptide
- EC
- 2.7.1.112
- UniProt
- P00524
- Ligands
- CO
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Src tyrosine kinase (EC 2.7.1.112) | protein | 96 | 17% helix, 31% strand | P00524 |
| B | Pqpyeeipi peptide | protein | 8 | 0% helix, 0% strand | — |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 507 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 1KC2 · structure of the triple (Lys(beta)D3Ala, Asp(beta)C8Ala, AspCD2Ala) mutant of the Src SH2… · the same entry in another collection · chain A against A, 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 P00524
- Elsewhere: RCSB PDB 1KC2 · PDBe 1KC2 · UniProt P00524
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