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Structure of the hsod A4V mutant

Analyse Structure of the hsod A4V mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1N19
Type: protein
Length: 306 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Superoxide dismutase [cu-zn]
EC: 1.15.1.1
UniProt: P00441
Ligands: CU1, ZN, SO4
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	153	8% helix, 39% strand	P00441

Ligands and binding sites

CU1 · Copper (I) ion · metal · 2 copies · chains A, B
ZN · Zinc ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · chains 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	183	0.64	0.85	34	empty
2	104	0.35	0.74	17	empty

Interfaces

1 interface between chains.

A–B · 740 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1N19 · Structure of the HSOD A4V mutant · 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 1N19 · PDBe 1N19 · UniProt P00441

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