MolNFT v1 · #133387 · protein
INPP5D pandda analysis group deposition -- crystal structure of the phosphatase and C2 domains of SHIP1 in complex with Z2856434829
5RXA: “INPP5D pandda analysis group deposition -- crystal structure of the phosphatase and C2 domains of SHIP1 in…”. X-ray diffraction, 1 ligand (ELQ). MolNFT v1 #133387 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5RXA
- Type
- protein
- Length
- 460 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q92835
- Ligands
- ELQ
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 460 | — | Q92835 |
Ligands and binding sites
- ELQ · [3,4-bis(fluoranyl)phenyl]-(4-methylpiperazin-1-yl)methanone · ligand · 2 copies · chains A
- DMS · Dimethyl sulfoxide · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q92835
- Elsewhere: RCSB PDB 5RXA · PDBe 5RXA · UniProt Q92835
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