MolNFT v1 · #15231 · protein

The 1.6 a structure of fe-superoxide dismutase from the thermophilic cyanobacterium thermosynechococcus elongatus : correlation of epr and structural characteristics

1MY6 · Iron (III) superoxide dismutase: “The 1.6 a structure of fe-superoxide dismutase from the thermophilic cyanobacterium thermosynechococcus…”. X-ray diffraction, 1 ligand (FE), 3 pockets (best druggability 0.54). MolNFT v1 #15231 on…

PDB: 1MY6
Type: protein
Length: 396 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Iron (III) superoxide dismutase
EC: 1.15.1.1
UniProt: Q8DIR2
Ligands: FE
Pockets: 3 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Iron (III) superoxide dismutase (EC 1.15.1.1)	protein	198	57% helix, 13% strand	Q8DIR2

Ligands and binding sites

FE · Fe (III) ion · metal · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	230	0.54	0.77	21	empty
2	226	0.54	0.77	24	empty
3	53	0.29	0.74	19	empty

Interfaces

1 interface between chains.

A–B · 942 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

1MY6 · The 1.6 A Structure of Fe-Superoxide Dismutase from the thermophilic cyanobacterium… · 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 Q8DIR2
Elsewhere: RCSB PDB 1MY6 · PDBe 1MY6 · UniProt Q8DIR2

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