Research workbench
Solution NMR structure of N-terminal domain (SH2 domain) of human inositol polyphosphate phosphatase-like protein 1 (INPPL1) (fragment 20-117), northeast structural genomics consortium target HR9134A
Analyse Solution NMR structure of N-terminal domain (SH2 domain) of human inositol… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MK2
- Type
- protein
- Length
- 109 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
- EC
- 3.1.3.86
- UniProt
- O15357
Structure
solution nmr · 1 distinct chain · 17% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) | protein | 109 | 17% helix, 25% strand | O15357 |
Compared structures
- 2MK2 · Solution NMR structure of N-terminal domain (SH2 domain) of human Inositol polyphosphate… · the same entry in another collection · chain A against A, TM-score 1.00
- O15357 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 3,4,5-trisphosphate… · a predicted model of the same protein · chain A against A, TM-score 0.82
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 O15357
- Elsewhere: RCSB PDB 2MK2 · PDBe 2MK2 · UniProt O15357
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