Research workbench
C-src (SH2 domain) complexed with ACE-phosphotyr-glu-(N-me(-(CH2)3- cyclopentyl))
Analyse C-src (SH2 domain) complexed with ACE-phosphotyr-glu-(N-me(-(CH2)3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1A1C
- Type
- protein
- Length
- 213 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P12931
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 105 | — | P12931 |
| B | — | protein | 104 | — | P12931 |
| C, D | — | protein | 2 | — | — |
Compared structures
- 1A1C · C-src (SH2 domain) complexed with ACE-phosphotyr-glu-(N-me(-(CH2)3-cyclopentyl)) · 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 1A1C · PDBe 1A1C · UniProt P12931
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