MolNFT v1 · #101072 · protein
The effects of lysine 200 and phenylalanine 239 farnesyl pyrophosphate synthase (fpps) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates
4NG6: “The effects of lysine 200 and phenylalanine 239 farnesyl pyrophosphate synthase (fpps) mutations on the…”. X-ray diffraction. MolNFT v1 #101072 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4NG6
- Type
- protein
- Length
- 344 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P14324
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 344 | — | P14324 |
Compared structures
- 4NG6 · The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS)… · the same entry in another collection · chain A against A, TM-score 1.00
- P14324 · AlphaFold monomer V2.0 prediction for farnesyl pyrophosphate synthase (P14324) · 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 P14324
- Elsewhere: RCSB PDB 4NG6 · PDBe 4NG6 · UniProt P14324
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