MolNFT v1 · #9046 · protein

Alteration of the co-substrate selectivity of deacetoxycephalosporin C synthase: the role of arginine-258

1HJG: “Alteration of the co-substrate selectivity of deacetoxycephalosporin C synthase: the role of arginine-258”. X-ray diffraction, 2 ligands (KIV, FE2), 1 pocket (best druggability 0.63). MolNFT v1 #9046 on GenesisL1: 3D structure…

PDB: 1HJG
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Deacetoxycephalosporin C synthase
UniProt: P18548
Ligands: KIV, FE2
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Deacetoxycephalosporin C synthase	protein	264	33% helix, 26% strand	P18548

Ligands and binding sites

KIV · 3-methyl-2-oxobutanoic acid · ligand · chains A
FE2 · Fe (II) ion · metal · 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	170	0.63	0.84	36	KIV

Compared structures

1HJG · Alteration of the co-substrate selectivity of deacetoxycephalosporin C synthase: The role… · the same entry in another collection · chain A against A, TM-score 1.00
P18548 · AlphaFold monomer V2.0 prediction for deacetoxycephalosporin C synthase (P18548) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 P18548
Elsewhere: RCSB PDB 1HJG · PDBe 1HJG · UniProt P18548

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