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Lsfa from P. aeruginosa, a 1-cys prx in sulfonic acid form

Analyse Lsfa from P. aeruginosa, a 1-cys prx in sulfonic acid form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7KUU
Type: protein
Length: 406 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alkyl hydroperoxide reductase C
EC: 1.11.1.26
UniProt: A0A0H2ZEH5
Pockets: 7 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alkyl hydroperoxide reductase C (EC 1.11.1.26)	protein	205	32% helix, 26% strand	A0A0H2ZEH5
B	Alkyl hydroperoxide reductase C (EC 1.11.1.26)	protein	201	32% helix, 26% strand	A0A0H2ZEH5

Pockets

7 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	383	0.73	0.84	38	empty
2	62	0.42	0.81	15	empty
3	94	0.39	0.76	27	empty
4	50	0.37	0.80	13	empty
5	65	0.36	0.78	21	empty

Interfaces

1 interface between chains.

A–B · 2002 Å² buried · 25 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

7KUU · LsfA from P. aeruginosa, a 1-Cys Prx in Sulfonic acid form · 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 A0A0H2ZEH5
Elsewhere: RCSB PDB 7KUU · PDBe 7KUU · UniProt A0A0H2ZEH5

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