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Structure of yiht from salmonella typhimurium

Analyse Structure of yiht from salmonella typhimurium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TO3
Type: protein
Length: 291 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative aldolase yiht
EC: 4.1.-.-
UniProt: Q9L7R9
Ligands: BR, PO4
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative aldolase yiht (EC 4.1.-.-)	protein	291	45% helix, 19% strand	Q9L7R9

Ligands and binding sites

BR · Bromide ion · ion · 9 copies · chains A
PO4 · Phosphate ion · ion · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	319	0.65	0.81	40	PO4, BR
2	50	0.34	0.79	10	empty

Modifications

Observed in the structure: 11 modified (engineered).

Compared structures

1TO3 · Structure of yiht from Salmonella typhimurium · the same entry in another collection · chain A against A, TM-score 1.00
Q9L7R9 · AlphaFold monomer V2.0 prediction for sulfofructosephosphate aldolase (Q9L7R9) · a predicted model of the same protein · 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 Q9L7R9
Elsewhere: RCSB PDB 1TO3 · PDBe 1TO3 · UniProt Q9L7R9

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