MolNFT v1 · #266 · protein
C-src (SH2 domain) complexed with ACE-phosphotyr-glu-(3- butylpiperidine)
1A1E · C-src tyrosine kinase: “C-src (SH2 domain) complexed with ACE-phosphotyr-glu-(3- butylpiperidine)”. X-ray diffraction, 2 ligands (ACE, DIY), 1 pocket (best druggability 0.52). MolNFT v1 #266 on GenesisL1: 3D structure, binding sites…
- PDB
- 1A1E
- Type
- protein
- Length
- 212 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-src tyrosine kinase; ACE-phosphotyr-glu-(3-butylpiperidine)
- EC
- 2.7.1.112
- UniProt
- P12931
- Ligands
- ACE, DIY
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | C-src tyrosine kinase (EC 2.7.1.112) | protein | 104 | 17% helix, 29% strand | P12931 |
| C, D | ACE-phosphotyr-glu-(3-butylpiperidine) | protein | 2 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, B, C, D
- DIY · 5-butylpiperidine · ligand · 2 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.52 | 0.78 | 26 | ACE |
Interfaces
4 interfaces between chains.
- A–B · 521 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 303 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 300 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 72 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent, 2 modified (covalent ligand, phosphorylation).
Compared structures
- 1A1E · C-src (SH2 domain) complexed with ACE-phosphotyr-glu-(3-butylpiperidine) · 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 P12931
- Elsewhere: RCSB PDB 1A1E · PDBe 1A1E · UniProt P12931
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