MolNFT v1 · #136145 · protein
Crystal structure of triosephosphate isomerase from francisella tularensis subsp. tularensis schu S4
5UJW: “Crystal structure of triosephosphate isomerase from francisella tularensis subsp. tularensis schu S4”. X-ray diffraction, 1 ligand (13P). MolNFT v1 #136145 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5UJW
- Type
- protein
- Length
- 1,482 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5NII7
- Ligands
- 13P
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 247 | — | Q5NII7 |
| B | — | protein | 243 | — | Q5NII7 |
| C, E | — | protein | 248 | — | Q5NII7 |
| D | — | protein | 250 | — | Q5NII7 |
| F | — | protein | 246 | — | Q5NII7 |
Ligands and binding sites
- 13P · 1,3-dihydroxyacetonephosphate · ligand · 2 copies · chains A, C
- IPA · Isopropyl alcohol · additive · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · chains C
- CIT · Citric acid · additive · chains D
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 Q5NII7
- Elsewhere: RCSB PDB 5UJW · PDBe 5UJW · UniProt Q5NII7
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