MolNFT v1 · #189168 · protein

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

7V4O · Beta-hydroxylase: “Unique non-heme hydroxylase in biosynthesis of nucleoside antibiotic pathway uncover mechanism of reaction”. X-ray diffraction, 1 ligand (P3G), 3 pockets (best druggability 0.72). MolNFT v1 #189168 on GenesisL1…

PDB: 7V4O
Type: protein
Length: 352 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-hydroxylase
UniProt: C4NCJ7
Ligands: P3G
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Beta-hydroxylase	protein	176	23% helix, 33% strand	C4NCJ7

Ligands and binding sites

P3G · 3,6,9,12,15-pentaoxaheptadecane · ligand · 2 copies · chains B, A

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

Pockets

3 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	401	0.72	0.83	49	P3G
2	289	0.71	0.85	38	P3G
3	106	0.37	0.74	23	empty

Interfaces

1 interface between chains.

B–A · 513 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

7V4O · Unique non-heme hydroxylase in biosynthesis of nucleoside antibiotic pathway uncover… · the same entry in another collection · chain B against B, 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 7V4O · PDBe 7V4O · UniProt C4NCJ7

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