Research workbench
Fha domain from human CHK2 kinase in complex with a synthetic phosphopeptide
Analyse Fha domain from human CHK2 kinase in complex with a synthetic phosphopeptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GXC
- Type
- protein
- Length
- 496 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O96017
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, J | — | protein | 116 | — | O96017 |
| B, E, H, K | — | protein | 8 | — | — |
Compared structures
- 1GXC · FHA domain from human Chk2 kinase in complex with a synthetic phosphopeptide · the same entry in another collection · chain K against K, TM-score 1.00
- O96017 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase CHK2 (O96017) · a predicted model of the same protein · chain D against A, TM-score 0.98
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 O96017
- Elsewhere: RCSB PDB 1GXC · PDBe 1GXC · UniProt O96017
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