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Structure of mycobacterium tuberculosis triosephosphate isomerase

Analyse Structure of mycobacterium tuberculosis triosephosphate isomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TA6
Type: protein
Length: 511 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Triosephosphate isomerase
EC: 5.3.1.1
UniProt: P66940
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Triosephosphate isomerase (EC 5.3.1.1)	protein	255	49% helix, 15% strand	P66940
B	Triosephosphate isomerase (EC 5.3.1.1)	protein	256	48% helix, 14% strand	P66940

Ligands and binding sites

FLC · Citrate anion · additive · chains A, B

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	173	0.59	0.82	34	FLC
2	117	0.41	0.76	27	empty
3	85	0.38	0.77	24	empty

Interfaces

1 interface between chains.

A–B · 1765 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

3TA6 · Structure of Mycobacterium tuberculosis triosephosphate isomerase · the same entry in another collection · 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 P66940
Elsewhere: RCSB PDB 3TA6 · PDBe 3TA6 · UniProt P66940

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