Research workbench
The structure of HFAM20C and HFAM20A complex
Analyse The structure of HFAM20C and HFAM20A complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YH3
- Type
- protein
- Length
- 1,575 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q96MK3, Q8IXL6
- Ligands
- ATP
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 438 | — | Q96MK3 |
| C | — | protein | 385 | — | Q8IXL6 |
| D | — | protein | 314 | — | Q8IXL6 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5YH3 · The structure of hFam20C and hFam20A complex · the same entry in another collection · chain D against D, TM-score 1.00
- Q8IXL6 · AlphaFold monomer V2.0 prediction for extracellular SERINE/THREONINE protein kinase… · a predicted model of the same protein · chain C against A, TM-score 1.00
- Q96MK3 · AlphaFold monomer V2.0 prediction for pseudokinase FAM20A (Q96MK3) · a predicted model of the same protein · chain B 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 Q96MK3
- Every structure of UniProt Q8IXL6
- Elsewhere: RCSB PDB 5YH3 · PDBe 5YH3 · UniProt Q96MK3 · UniProt Q8IXL6
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