MolNFT v1 · #33485 · protein
Crystal structure of the catalytic domain of serine threonine protein phosphatase pstp in complex with 2 manganese ions.
2CM1: “Crystal structure of the catalytic domain of serine threonine protein phosphatase pstp in complex with 2…”. X-ray diffraction, 1 ligand (MN), 1 pocket (best druggability 0.35). MolNFT v1 #33485 on GenesisL1: 3D structure, binding…
- PDB
- 2CM1
- Type
- protein
- Length
- 230 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine threonine protein phosphatase pstp
- EC
- 3.1.3.16
- UniProt
- P71588
- Ligands
- MN
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine threonine protein phosphatase pstp (EC 3.1.3.16) | protein | 230 | 32% helix, 31% strand | P71588 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.35 | 0.76 | 19 | empty |
Compared structures
- 2CM1 · Crystal structure of the catalytic domain of serine threonine protein phosphatase PstP in… · the same entry in another collection · chain A against A, 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 P71588
- Elsewhere: RCSB PDB 2CM1 · PDBe 2CM1 · UniProt P71588
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