MolNFT v1 · #189169 · protein

Unique non-heme hydroxylase in biosynthesis of nucleoside antibiotic pathway uncover mechanism of reaction

7V4P · Beta-hydroxylase: “Unique non-heme hydroxylase in biosynthesis of nucleoside antibiotic pathway uncover mechanism of reaction”. X-ray diffraction, 1 ligand (FE), 2 pockets (best druggability 0.79). MolNFT v1 #189169 on GenesisL1: 3D…

PDB: 7V4P
Type: protein
Length: 336 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-hydroxylase
UniProt: C4NCJ7
Ligands: FE
Pockets: 2 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Beta-hydroxylase	protein	168	15% helix, 35% strand	C4NCJ7

Ligands and binding sites

FE · Fe (III) ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	883	0.79	0.82	68	empty
2	332	0.70	0.83	31	empty

Interfaces

1 interface between chains.

A–B · 438 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

7V4P · Unique non-heme hydroxylase in biosynthesis of nucleoside antibiotic pathway uncover… · 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 C4NCJ7
Elsewhere: RCSB PDB 7V4P · PDBe 7V4P · UniProt C4NCJ7

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