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Structure-function in E. COLI iron superoxide dismutase: comparisons with the manganese enzyme from T. thermophilus

Analyse Structure-function in E. COLI iron superoxide dismutase: comparisons with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ISC
Type: protein
Length: 384 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: P09157
Ligands: FE, AZI
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	IRON(III) superoxide dismutase (EC 1.15.1.1)	protein	192	53% helix, 12% strand	P09157

Ligands and binding sites

FE · Fe (III) ion · metal · 2 copies · chains A, B
AZI · Azide ion · ion · 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	188	0.56	0.80	20	empty
2	187	0.55	0.79	20	empty

Interfaces

1 interface between chains.

A–B · 982 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

1ISC · Structure-function in E. COLI iron superoxide dismutase: comparisons with the manganese… · 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 P09157
Elsewhere: RCSB PDB 1ISC · PDBe 1ISC · UniProt P09157

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