Research workbench
Crystal structure analysis of kinase associated phosphatase (kap) with a substitution of the catalytic site cysteine (CYS140) to a serine
Analyse Crystal structure analysis of kinase associated phosphatase (kap) with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FPZ
- Type
- protein
- Length
- 1,062 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q16667
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E | — | protein | 176 | — | Q16667 |
| C, D, F | — | protein | 178 | — | Q16667 |
Compared structures
- 1FPZ · Crystal structure analysis of kinase associated phosphatase (kap) with a substitution of… · the same entry in another collection · chain F against F, TM-score 1.00
- Q16667 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase inhibitor 3 (Q16667) · a predicted model of the same protein · chain E against A, TM-score 0.99
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 Q16667
- Elsewhere: RCSB PDB 1FPZ · PDBe 1FPZ · UniProt Q16667
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