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The first ketoreductase of the erythromycin synthase (crystal form 1)

Analyse The first ketoreductase of the erythromycin synthase (crystal form 1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FR0
Type: protein
Length: 468 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Erythromycin synthase, eryai
EC: 1.1.1.100
UniProt: Q03131
Ligands: NDP
Pockets: 6 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Erythromycin synthase, eryai (EC 1.1.1.100)	protein	468	37% helix, 21% strand	Q03131

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	306	0.71	0.85	41	empty
2	456	0.68	0.79	42	NDP
3	138	0.57	0.82	20	empty
4	129	0.45	0.77	25	empty
5	98	0.42	0.78	25	empty

Compared structures

2FR0 · The first ketoreductase of the erythromycin synthase (crystal form 1) · 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 Q03131
Elsewhere: RCSB PDB 2FR0 · PDBe 2FR0 · UniProt Q03131

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