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Crystal structure of superoxide dismutase from P. marinus

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

PDB: 2CW2
Type: protein
Length: 395 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Superoxide dismutase 1
EC: 1.15.1.1
UniProt: Q8ISJ0
Ligands: FE
Pockets: 2 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 54% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Superoxide dismutase 1 (EC 1.15.1.1)	protein	199	53% helix, 12% strand	Q8ISJ0
B	Superoxide dismutase 1 (EC 1.15.1.1)	protein	196	56% helix, 13% strand	Q8ISJ0

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

2 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	239	0.58	0.79	21	empty
2	216	0.55	0.78	20	empty

Interfaces

1 interface between chains.

A–B · 994 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

2CW2 · Crystal structure of Superoxide dismutase from P. 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 Q8ISJ0
Elsewhere: RCSB PDB 2CW2 · PDBe 2CW2 · UniProt Q8ISJ0

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