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Neutron structure of reduced human mnsod

Analyse Neutron structure of reduced human mnsod in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7KKW
Type: protein
Length: 398 residues
Chains: 2
Method: neutron diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Superoxide dismutase [mn], mitochondrial
EC: 1.15.1.1
UniProt: P04179
Ligands: MN
Pockets: 2 · best druggability 0.32

Structure

neutron diffraction · 1 distinct chain · 59% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Superoxide dismutase [mn], mitochondrial (EC 1.15.1.1)	protein	199	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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	75	0.32	0.74	18	empty
2	67	0.31	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 1075 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

7KKW · Neutron structure of Reduced Human MnSOD · 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 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 P04179
Elsewhere: RCSB PDB 7KKW · PDBe 7KKW · UniProt P04179

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