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Type II dehydroquinase from mycobacterium tuberculosis complexed with 2,3-anhydro-quinic acid

Analyse Type II dehydroquinase from mycobacterium tuberculosis complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H0R
Type: protein
Length: 139 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-dehydroquinate dehydratase
EC: 4.2.1.10
UniProt: P36918
Ligands: FA1, CL, PO4
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-dehydroquinate dehydratase (EC 4.2.1.10)	protein	139	43% helix, 18% strand	P36918

Ligands and binding sites

FA1 · 2,3 -anhydro-quinic acid · ligand · chains A
CL · Chloride ion · ion · 2 copies · chains A
PO4 · Phosphate ion · ion · chains A
GOL · Glycerol · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	88	0.48	0.82	20	FA1

Compared structures

1H0R · Type II Dehydroquinase from Mycobacterium tuberculosis complexed with 2,3-anhydro-quinic… · 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 P36918
Elsewhere: RCSB PDB 1H0R · PDBe 1H0R · UniProt P36918

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