MolNFT v1 · #120497 · protein

Crystal structure of the NTD_N/C domain of alkylhydroperoxide reductase ahpf from enterococcus faecalis (V583)

5H29 · Thioredoxin REDUCTASE/GLUTATHIONE-related protein: “Crystal structure of the NTD_N/C domain of alkylhydroperoxide reductase ahpf from enterococcus faecalis (V583)”. X-ray diffraction, 2 ligands (PRO, SO4), 3 pockets (best…

PDB: 5H29
Type: protein
Length: 207 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin REDUCTASE/GLUTATHIONE-related protein
UniProt: Q830N9
Ligands: PRO, SO4
Pockets: 3 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin REDUCTASE/GLUTATHIONE-related protein	protein	207	42% helix, 23% strand	Q830N9

Ligands and binding sites

PRO · Proline · ligand · chains A
SO4 · Sulfate ion · ion · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	70	0.37	0.78	21	empty
2	70	0.30	0.74	23	empty
3	63	0.28	0.73	17	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5H29 · Crystal Structure of the NTD_N/C domain of Alkylhydroperoxide Reductase AhpF from… · 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 5H29 · PDBe 5H29 · UniProt Q830N9

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