MolNFT v1 · #154956 · protein
Crystal structure of ATPTP1 at 1.4 ångström
6KRW · Protein-tyrosine-phosphatase PTP1: “Crystal structure of ATPTP1 at 1.4 ångström”. X-ray diffraction, 1 ligand (IOD), 3 pockets (best druggability 0.51). MolNFT v1 #154956 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6KRW
- Type
- protein
- Length
- 306 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein-tyrosine-phosphatase PTP1
- EC
- 3.1.3.48
- UniProt
- O82656
- Ligands
- IOD
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-tyrosine-phosphatase PTP1 (EC 3.1.3.48) | protein | 306 | 41% helix, 17% strand | O82656 |
Ligands and binding sites
- IOD · Iodide ion · ion · 3 copies · chains A
- FLC · Citrate anion · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 187 | 0.51 | 0.77 | 30 | IOD, FLC, PEG |
| 2 | 74 | 0.35 | 0.76 | 14 | empty |
| 3 | 50 | 0.31 | 0.77 | 13 | empty |
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 O82656
- Elsewhere: RCSB PDB 6KRW · PDBe 6KRW · UniProt O82656
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