Research workbench
Catalytic domain of human SERINE/THREONINE phosphatase 5 (PP5C)WITH two ZN2+ atoms originally soaked with cantharidin (which is present in the structure in the hydrolyzed form)
Analyse Catalytic domain of human SERINE/THREONINE phosphatase 5 (PP5C)WITH two ZN2+… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H68
- Type
- protein
- Length
- 630 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P53041
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 315 | — | P53041 |
Compared structures
- 3H68 · Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Zn2+ atoms… · the same entry in another collection · chain A against A, TM-score 1.00
- P53041 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase 5 (P53041) · a predicted model of the same protein · 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 P53041
- Elsewhere: RCSB PDB 3H68 · PDBe 3H68 · UniProt P53041
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