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Tetracenomycin ARO/CYC nai structure

Analyse Tetracenomycin ARO/CYC nai structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2REZ
Type: protein
Length: 155 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Multifunctional cyclase-dehydratase-3-O-methyl transferase tcmn
UniProt: P16559
Ligands: IOD
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Multifunctional cyclase-dehydratase-3-O-methyl transferase tcmn	protein	155	29% helix, 41% strand	P16559

Ligands and binding sites

IOD · Iodide ion · ion · 5 copies · chains A
ACT · Acetate ion · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	119	0.80	0.98	30	ACT, IOD
2	53	0.35	0.78	18	ACT, IOD

Compared structures

2REZ · Tetracenomycin ARO/CYC NaI Structure · the same entry in another collection · chain A against A, TM-score 1.00
P16559 · AlphaFold monomer V2.0 prediction for multifunctional cyclase- dehydratase-3-O-methyl… · a predicted model of the same protein · chain A against A, TM-score 0.92

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 P16559
Elsewhere: RCSB PDB 2REZ · PDBe 2REZ · UniProt P16559

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