MolNFT v1 · #115324 · protein

Leishmania siamensis triosephosphate isomerase

5CG7: “Leishmania siamensis triosephosphate isomerase”. X-ray diffraction, 6 pockets (best druggability 0.48). MolNFT v1 #115324 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5CG7
Type: protein
Length: 491 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Triosephosphate isomerase
EC: 5.3.1.1
UniProt: I2APN2
Pockets: 6 · best druggability 0.48

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Triosephosphate isomerase (EC 5.3.1.1)	protein	245	47% helix, 16% strand	I2APN2
B	Triosephosphate isomerase (EC 5.3.1.1)	protein	246	47% helix, 16% strand	I2APN2

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	182	0.48	0.76	23	empty
2	177	0.46	0.75	39	empty
3	130	0.46	0.78	24	empty
4	90	0.42	0.78	14	empty
5	109	0.42	0.77	24	empty

Interfaces

1 interface between chains.

A–B · 293 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (artifact).

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 I2APN2
Elsewhere: RCSB PDB 5CG7 · PDBe 5CG7 · UniProt I2APN2

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