Research workbench

Human manganese superoxide dismutase mutant Q143N

Analyse Human manganese superoxide dismutase mutant Q143N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QNM
Type: protein
Length: 396 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Manganese superoxide dismutase
EC: 1.15.1.1
UniProt: P04179
Ligands: MN
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Manganese superoxide dismutase (EC 1.15.1.1)	protein	198	59% helix, 13% strand	P04179

Ligands and binding sites

MN · Manganese (II) ion · metal · 2 copies · chains A, B

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

Pockets

2 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	176	0.51	0.78	22	empty
2	171	0.49	0.77	22	empty

Interfaces

1 interface between chains.

A–B · 895 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

1QNM · Human manganese superoxide dismutase mutant Q143N · the same entry in another collection · chain A against A, TM-score 1.00
P04179 · AlphaFold monomer V2.0 prediction for superoxide dismutase [mn], mitochondrial (P04179) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P04179
Elsewhere: RCSB PDB 1QNM · PDBe 1QNM · UniProt P04179

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