Research workbench
Acanthamoeba igpd in complex with R-C348 to 1.7A resolution
Analyse Acanthamoeba igpd in complex with R-C348 to 1.7A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FWH
- Type
- protein
- Length
- 2,338 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1P7ZJC8
- Ligands
- 5LD, MN, MG
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 196 | — | A0A1P7ZJC8 |
| B, C, D, F, G, H, K, L | — | protein | 195 | — | A0A1P7ZJC8 |
| E, I, J | — | protein | 194 | — | A0A1P7ZJC8 |
Ligands and binding sites
- 5LD · [(2R)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)propyl]phosphonic acid · ligand · 12 copies · chains A, C, F, B, K, G, L, E, D, H, J, I
- MN · Manganese (II) ion · metal · 24 copies · chains A, F, B, G, C, J, D, L, E, K, H, I
- MG · Magnesium ion · metal · chains L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FWH · Acanthamoeba IGPD in complex with R-C348 to 1.7A resolution · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A1P7ZJC8
- Elsewhere: RCSB PDB 6FWH · PDBe 6FWH · UniProt A0A1P7ZJC8
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