Research workbench

Peroxiredoxin from aeropyrum pernix K1 (apprx) 0CYS W210A mutant

Analyse Peroxiredoxin from aeropyrum pernix K1 (apprx) 0CYS W210A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KRR
Type: protein
Length: 976 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peroxiredoxin
EC: 1.11.1.15
UniProt: Q9Y9L0
Pockets: 11 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Peroxiredoxin (EC 1.11.1.15)	protein	244	33% helix, 24% strand	Q9Y9L0

Pockets

11 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	247	0.50	0.75	37	empty
2	209	0.49	0.75	37	empty
3	212	0.49	0.75	37	empty
4	191	0.47	0.75	35	empty
5	202	0.42	0.72	30	empty

Interfaces

5 interfaces between chains.

C–D · 3533 Å² buried · 60 hydrogen bonds · protein-protein
A–B · 3532 Å² buried · 60 hydrogen bonds · protein-protein
A–C · 486 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 23 Å² buried · 0 hydrogen bonds · protein-protein
A–D · 14 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6KRR · Peroxiredoxin from Aeropyrum pernix K1 (ApPrx) 0Cys W210A mutant · 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 Q9Y9L0
Elsewhere: RCSB PDB 6KRR · PDBe 6KRR · UniProt Q9Y9L0

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