MolNFT v1 · #121611 · protein

Insights into substrate modification by dehydratases from type I polyketide synthases

5I0K · Phthiocerol synthesis polyketide synthase type I ppsc: “Insights into substrate modification by dehydratases from type I polyketide synthases”. X-ray diffraction, 1 ligand (COO), 1 pocket (best druggability 0.75). MolNFT v1 #121611…

PDB: 5I0K
Type: protein
Length: 265 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: COO
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phthiocerol synthesis polyketide synthase type I ppsc (EC 2.3.1.41)	protein	265	18% helix, 37% strand	P96202

Ligands and binding sites

COO · Crotonyl coenzyme A · ligand · 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	281	0.75	0.88	40	empty

Compared structures

5I0K · Insights into Substrate Modification by Dehydratases from Type I Polyketide Synthases · 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 0.96

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 5I0K · PDBe 5I0K · UniProt P96202

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