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Solution structure of disulfide reduced and copper depleted human superoxide dismutase

Analyse Solution structure of disulfide reduced and copper depleted human superoxide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AF2
Type: protein
Length: 306 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Superoxide dismutase [cu-zn]
EC: 1.15.1.1
UniProt: P00441
Ligands: ZN
Pockets: 2 · best druggability 0.45

Structure

solution nmr · 1 distinct chain · 3% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	153	3% helix, 37% strand	P00441

Ligands and binding sites

ZN · Zinc 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	150	0.45	0.76	29	empty
2	73	0.38	0.78	20	empty

Interfaces

1 interface between chains.

A–B · 1005 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

2AF2 · Solution structure of disulfide reduced and copper depleted Human Superoxide Dismutase · 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 P00441
Elsewhere: RCSB PDB 2AF2 · PDBe 2AF2 · UniProt P00441

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