Research workbench
Crystal structure of the C-src-SH3 domain Q128R mutant in complex with the high affinity peptide APP12
Analyse Crystal structure of the C-src-SH3 domain Q128R mutant in complex with the high… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OB1
- Type
- protein
- Length
- 69 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proto-oncogene tyrosine-protein kinase src; APP12
- EC
- 2.7.10.2
- UniProt
- P00523
- Ligands
- ACE
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proto-oncogene tyrosine-protein kinase src (EC 2.7.10.2) | protein | 57 | 5% helix, 46% strand | P00523 |
| B | APP12 | protein | 12 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 559 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 5OB1 · Crystal structure of the c-Src-SH3 domain Q128R mutant in complex with the high affinity… · 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 P00523
- Elsewhere: RCSB PDB 5OB1 · PDBe 5OB1 · UniProt P00523
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