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Crystal structure of triosephosphate isomerase from francisella tularensis subsp. tularensis schu S4

Analyse Crystal structure of triosephosphate isomerase from francisella tularensis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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.

Compared structures

5UJW · Crystal structure of triosephosphate isomerase from Francisella tularensis subsp.… · the same entry in another collection · chain F against F, TM-score 1.00
Q5NII7 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (Q5NII7) · a predicted model of the same protein · chain B against A, TM-score 0.98

Analyse

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Every structure of UniProt Q5NII7
Elsewhere: RCSB PDB 5UJW · PDBe 5UJW · UniProt Q5NII7

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