Research workbench
Structure of the N-SH2 domain of the human tyrosine-protein phosphatase non-receptor type 11 in complex with the phosphorylated immune receptor tyrosine-based switch motif
Analyse Structure of the N-SH2 domain of the human tyrosine-protein phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ROZ
- Type
- protein
- Length
- 224 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase non-receptor type 11; Immune receptor tyrosine-based switch…
- EC
- 3.1.3.48
- UniProt
- Q06124
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Tyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48) | protein | 102 | 24% helix, 29% strand | Q06124 |
| B, D | Immune receptor tyrosine-based switch motif (itsm) | protein | 10 | 0% helix, 30% strand | — |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 89 | 0.43 | 0.79 | 16 | empty |
| 2 | 61 | 0.32 | 0.76 | 16 | empty |
Interfaces
3 interfaces between chains.
- C–D · 652 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 631 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 274 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 6ROZ · Structure of the N-SH2 domain of the human tyrosine-protein phosphatase non-receptor type… · the same entry in another collection · chain B against B, 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 Q06124
- Elsewhere: RCSB PDB 6ROZ · PDBe 6ROZ · UniProt Q06124
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