MolNFT v1 · #95391 · protein

High-resolution structure of triosephosphate isomerase from E. COLI

4IOT: “High-resolution structure of triosephosphate isomerase from E. COLI”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.67). MolNFT v1 #95391 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4IOT
Type: protein
Length: 508 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Triosephosphate isomerase
EC: 5.3.1.1
UniProt: B1XB85
Ligands: SO4
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Triosephosphate isomerase (EC 5.3.1.1)	protein	254	50% helix, 16% strand	B1XB85

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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

Pockets

3 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	274	0.67	0.83	45	empty
2	119	0.45	0.78	26	SO4
3	73	0.38	0.78	19	empty

Interfaces

1 interface between chains.

A–B · 1708 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

4IOT · High-resolution Structure of Triosephosphate isomerase from E. coli · the same entry in another collection · chain A against A, TM-score 1.00
B1XB85 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (B1XB85) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 B1XB85
Elsewhere: RCSB PDB 4IOT · PDBe 4IOT · UniProt B1XB85

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