Research workbench
Lmfpps mutant T164Y in complex with 476A, ipp & ca
Analyse Lmfpps mutant T164Y in complex with 476A, ipp & ca in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VJC
- Type
- protein
- Length
- 724 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q4QBL1
- Ligands
- IPR, 476, CA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 362 | — | Q4QBL1 |
Ligands and binding sites
- IPR · Isopentyl pyrophosphate · ligand · 2 copies · chains A, B
- 476 · 3-butyl-1-(2,2-diphosphonoethyl)pyridinium · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 6 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q4QBL1
- Elsewhere: RCSB PDB 6VJC · PDBe 6VJC · UniProt Q4QBL1
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