Research workbench
Crystal structure of the C-src SH3 domain mutant V111L-N113S-T114S at pH 7.0
Analyse Crystal structure of the C-src SH3 domain mutant V111L-N113S-T114S at pH 7.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7A35
- Type
- protein
- Length
- 120 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proto-oncogene tyrosine-protein kinase src
- EC
- 2.7.10.2
- UniProt
- P00523
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Proto-oncogene tyrosine-protein kinase src (EC 2.7.10.2) | protein | 60 | 5% helix, 42% strand | P00523 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 106 | 0.37 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 325 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 7A35 · Crystal structure of the c-Src SH3 domain mutant V111L-N113S-T114S at pH 7.0 · 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 7A35 · PDBe 7A35 · UniProt P00523
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