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Structural and functional analysis of tetracenomycin F2 cyclase from streptomyces glaucescens: a type-II polyketide cyclase

Analyse Structural and functional analysis of tetracenomycin F2 cyclase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TUW
Type: protein
Length: 106 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tetracenomycin polyketide synthesis protein tcmi
UniProt: P39890
Ligands: SO4
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tetracenomycin polyketide synthesis protein tcmi	protein	106	38% helix, 26% strand	P39890

Ligands and binding sites

SO4 · Sulfate 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	271	0.73	0.86	29	SO4

Compared structures

1TUW · Structural and Functional Analysis of Tetracenomycin F2 Cyclase from Streptomyces… · the same entry in another collection · chain A against A, TM-score 1.00
P39890 · AlphaFold monomer V2.0 prediction for tetracenomycin F2 cyclase (P39890) · 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 P39890
Elsewhere: RCSB PDB 1TUW · PDBe 1TUW · UniProt P39890

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