Research workbench
Crystal structure of mutant human geranylgeranyl pyrophosphate synthase (Y246D) in its apo form
Analyse Crystal structure of mutant human geranylgeranyl pyrophosphate synthase (Y246D)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C56
- Type
- protein
- Length
- 553 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O95749
- Ligands
- VT0
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 286 | — | O95749 |
| B | — | protein | 267 | — | O95749 |
Ligands and binding sites
- VT0 · {[(2-phenylthieno[2,3-d]pyrimidin-4-yl) amino]methylene}bis(phosphonic acid) · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6C56 · Crystal structure of mutant human geranylgeranyl pyrophosphate synthase (Y246D) in its… · the same entry in another collection · chain A against A, TM-score 1.00
- O95749 · AlphaFold monomer V2.0 prediction for geranylgeranyl pyrophosphate synthase (O95749) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 O95749
- Elsewhere: RCSB PDB 6C56 · PDBe 6C56 · UniProt O95749
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