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Dehydratase domain of the polyketide ppsc from mycobacterium tuberculosis

Analyse Dehydratase domain of the polyketide ppsc from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OOC
Type: protein
Length: 268 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phthiocerol synthesis polyketide synthase type I ppsc
EC: 2.3.1.41
UniProt: P96202
Ligands: PO4
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phthiocerol synthesis polyketide synthase type I ppsc (EC 2.3.1.41)	protein	268	19% helix, 43% strand	P96202

Ligands and binding sites

PO4 · Phosphate ion · ion · 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	161	0.76	0.92	29	PO4

Compared structures

4OOC · Dehydratase domain of the polyketide PpsC from Mycobacterium tuberculosis · the same entry in another collection · chain A against A, TM-score 1.00
P96202 · AlphaFold monomer V2.0 prediction for PHENOLPHTHIOCEROL/PHTHIOCEROL polyketide synthase… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P96202
Elsewhere: RCSB PDB 4OOC · PDBe 4OOC · UniProt P96202

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