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Structure of enterococcus faecalis (V583) alkylhydroperoxide reductase subunit F (ahpf) C503A mutant

Analyse Structure of enterococcus faecalis (V583) alkylhydroperoxide reductase subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IL7
Type: protein
Length: 208 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin REDUCTASE/GLUTATHIONE-related protein
UniProt: Q830N9
Ligands: SO4
Pockets: 2 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin REDUCTASE/GLUTATHIONE-related protein	protein	208	40% helix, 23% strand	Q830N9

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	50	0.35	0.80	14	empty
2	63	0.28	0.74	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6IL7 · Structure of Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit F (AhpF)… · 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 Q830N9
Elsewhere: RCSB PDB 6IL7 · PDBe 6IL7 · UniProt Q830N9

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