Research workbench
P130CAS SH3 domain ptp-pest peptide chimera
Analyse P130CAS SH3 domain ptp-pest peptide chimera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O2P
- Type
- protein
- Length
- 100 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Breast cancer anti-estrogen resistance 1,TYROSINE-protein phosphatase non-receptor type 12
- EC
- 3.1.3.48
- UniProt
- Q6P5Z4, Q05209
Structure
solution nmr · 1 distinct chain · 6% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Breast cancer anti-estrogen resistance 1,TYROSINE-protein phosphatase non-receptor type 12 (EC 3.1.3.48) | protein | 100 | 6% helix, 31% strand | Q6P5Z4, Q05209 |
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 Q6P5Z4
- Every structure of UniProt Q05209
- Elsewhere: RCSB PDB 5O2P · PDBe 5O2P · UniProt Q6P5Z4 · UniProt Q05209
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