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Mycobacterium tuberculosis epsp synthase in complex with intermediate

Analyse Mycobacterium tuberculosis epsp synthase in complex with intermediate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O0X
Type: protein
Length: 424 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-phosphoshikimate 1-carboxyvinyltransferase
EC: 2.5.1.19
UniProt: P22487
Ligands: SKP, SO4
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19)	protein	424	37% helix, 21% strand	P22487

Ligands and binding sites

SKP · 5-(1-carboxy-1-phosphonooxy-ethoxyl)-4-hydroxy-3-phosphonooxy-cyclohex-1-enecarboxylic acid · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	116	0.77	0.97	35	SKP

Compared structures

2O0X · Mycobacterium tuberculosis epsp synthase in complex with intermediate · 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 P22487
Elsewhere: RCSB PDB 2O0X · PDBe 2O0X · UniProt P22487

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