Research workbench
P56LCK SH2 domain inhibitor complex
Analyse P56LCK SH2 domain inhibitor complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BHF
- Type
- protein
- Length
- 109 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T-lymphocyte-specific protein tyrosine kinase P56LCK; Inhibitor ACE-ipa-glu-glu-ile
- EC
- 2.7.1.112
- UniProt
- P06239
- Ligands
- ACE
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-lymphocyte-specific protein tyrosine kinase P56LCK (EC 2.7.1.112) | protein | 105 | 17% helix, 30% strand | P06239 |
| I | Inhibitor ACE-ipa-glu-glu-ile | protein | 4 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–I · 465 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, nonstandard).
Compared structures
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 P06239
- Elsewhere: RCSB PDB 1BHF · PDBe 1BHF · UniProt P06239
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