MolNFT v1 · #107805 · protein

Crystal structure of a single mutant (N71D) of triosephosphate isomerase from human

4UNL: “Crystal structure of a single mutant (N71D) of triosephosphate isomerase from human”. X-ray diffraction, 3 pockets (best druggability 0.70). MolNFT v1 #107805 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4UNL
Type: protein
Length: 492 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Triosephosphate isomerase
EC: 5.3.1.1
UniProt: P60174
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Triosephosphate isomerase (EC 5.3.1.1)	protein	246	46% helix, 16% strand	P60174

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	55	0.70	0.98	16	empty
2	119	0.46	0.78	27	empty
3	89	0.40	0.77	19	empty

Interfaces

1 interface between chains.

A–B · 1786 Å² buried · 41 hydrogen bonds · protein-protein

Compared structures

4UNL · Crystal structure of a single mutant (N71D) of triosephosphate isomerase from human · the same entry in another collection · chain A against A, TM-score 1.00
P60174 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (P60174) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P60174
Elsewhere: RCSB PDB 4UNL · PDBe 4UNL · UniProt P60174

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