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Sphingobacterium sp. T2 manganese superoxide dismutase catalyses the oxidative demethylation of polymeric lignin via generation of hydroxyl radical

Analyse Sphingobacterium sp. T2 manganese superoxide dismutase catalyses the oxidative… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GSB
Type: protein
Length: 412 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Superoxide dismutase
EC: 1.15.1.1
UniProt: A0A0M3KL50
Ligands: MN
Pockets: 3 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Superoxide dismutase (EC 1.15.1.1)	protein	206	51% helix, 11% strand	A0A0M3KL50

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

3 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	178	0.48	0.76	18	empty
2	180	0.47	0.76	20	empty
3	59	0.27	0.73	13	empty

Interfaces

1 interface between chains.

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

Compared structures

6GSB · Sphingobacterium sp. T2 manganese superoxide dismutase catalyses the oxidative… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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Every structure of UniProt A0A0M3KL50
Elsewhere: RCSB PDB 6GSB · PDBe 6GSB · UniProt A0A0M3KL50

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