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Crystal structure of thermophilic tryptophan halogenase (th-hal) enzyme from streptomycin violaceusniger.

Analyse Crystal structure of thermophilic tryptophan halogenase (th-hal) enzyme from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LVA
Type: protein
Length: 346 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD(P)H-FMN oxidoreductase
UniProt: Q75V96
Ligands: FMN
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NAD(P)H-FMN oxidoreductase	protein	174	37% helix, 19% strand	Q75V96
B	NAD(P)H-FMN oxidoreductase	protein	172	37% helix, 18% strand	Q75V96

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	225	0.50	0.75	24	FMN
2	211	0.48	0.74	23	FMN

Interfaces

1 interface between chains.

A–B · 1258 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

5LVA · Crystal structure of thermophilic tryptophan halogenase (Th-Hal) enzyme from Streptomycin… · 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 Q75V96
Elsewhere: RCSB PDB 5LVA · PDBe 5LVA · UniProt Q75V96

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