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A nonheme iron- and alpha-ketoglutarate- dependent halogenase that catalyzes nucleotide substrates

Analyse A nonheme iron- and alpha-ketoglutarate- dependent halogenase that catalyzes… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7W5S
Type: protein
Length: 302 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nonheme iron and alpha-ketoglutarate dependent halogenase
UniProt: A0A1U8X168
Ligands: FE2, SO4, CL
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nonheme iron and alpha-ketoglutarate dependent halogenase	protein	302	31% helix, 27% strand	A0A1U8X168

Ligands and binding sites

FE2 · Fe (II) ion · metal · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A
CL · Chloride ion · ion · chains A
PEG · Di(hydroxyethyl)ether · additive · 7 copies · 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	407	0.70	0.81	60	FE2, CL

Compared structures

7W5S · A nonheme iron- and alpha-ketoglutarate- dependent halogenase that catalyzes nucleotide… · 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 A0A1U8X168
Elsewhere: RCSB PDB 7W5S · PDBe 7W5S · UniProt A0A1U8X168

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