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X-ray structure of PMSOD2, superoxide dismutase from perkinsus marinus

Analyse X-ray structure of PMSOD2, superoxide dismutase from perkinsus marinus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CW3
Type: protein
Length: 396 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Iron superoxide dismutase
EC: 1.15.1.1
UniProt: Q8ISI9
Ligands: FE
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Iron superoxide dismutase (EC 1.15.1.1)	protein	200	53% helix, 13% strand	Q8ISI9
B	Iron superoxide dismutase (EC 1.15.1.1)	protein	196	57% helix, 13% strand	Q8ISI9

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	224	0.59	0.80	21	empty
2	180	0.55	0.80	25	empty
3	77	0.32	0.74	19	empty

Interfaces

1 interface between chains.

A–B · 968 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

2CW3 · X-ray structure of PmSOD2, superoxide dismutase from Perkinsus marinus · 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 Q8ISI9
Elsewhere: RCSB PDB 2CW3 · PDBe 2CW3 · UniProt Q8ISI9

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