MolNFT v1 · #93427 · protein
Modulating the function of human serine racemase and human serine dehydratase by protein engineering
4H27 · L-serine DEHYDRATASE/L-threonine deaminase: “Modulating the function of human serine racemase and human serine dehydratase by protein engineering”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.64). MolNFT v1…
- PDB
- 4H27
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-serine DEHYDRATASE/L-threonine deaminase
- EC
- 4.3.1.17, 4.3.1.19
- UniProt
- P20132
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-serine DEHYDRATASE/L-threonine deaminase (EC 4.3.1.17, 4.3.1.19) | protein | 318 | 46% helix, 17% strand | P20132 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 475 | 0.64 | 0.77 | 49 | SO4 |
Modifications
Observed in the structure: 1 modified (cofactor).
Compared structures
- 4H27 · Modulating the function of human serine racemase and human serine dehydratase by protein… · the same entry in another collection · chain A against A, TM-score 1.00
- P20132 · AlphaFold monomer V2.0 prediction for L-serine DEHYDRATASE/L-threonine deaminase (P20132) · a predicted model of the same protein · chain A 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 P20132
- Elsewhere: RCSB PDB 4H27 · PDBe 4H27 · UniProt P20132
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