MolNFT v1 · #21895 · protein

Atomic structures of wild-type and thermostable mutant recombinant human cu, zn superoxide dismutase

1SOS: “Atomic structures of wild-type and thermostable mutant recombinant human cu, zn superoxide dismutase”. X-ray diffraction, 4 ligands (ACE, CU, ZN), 17 pockets (best druggability 0.80). MolNFT v1 #21895 on GenesisL1: 3D structure…

PDB: 1SOS
Type: protein
Length: 1,530 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Superoxide dismutase
EC: 1.15.1.1
UniProt: P00441
Ligands: ACE, CU, ZN, SO4
Pockets: 17 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, F, B, G, C, H, D, I, E, J	Superoxide dismutase (EC 1.15.1.1)	protein	153	6% helix, 41% strand	P00441

Ligands and binding sites

ACE · Acetyl group · ligand · 10 copies · chains A, F, B, G, C, H, D, I, E, J
CU · Copper (II) ion · metal · 10 copies · chains A, F, B, G, C, H, D, I, E, J
ZN · Zinc ion · metal · 10 copies · chains A, F, B, G, C, H, D, I, E, J
SO4 · Sulfate ion · ion · 2 copies · chains F, G, H, I, J

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

17 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	894	0.80	0.82	94	empty
2	912	0.74	0.78	94	SO4
3	465	0.74	0.83	62	empty
4	755	0.71	0.77	68	empty
5	246	0.63	0.82	33	empty

Interfaces

13 interfaces between chains.

E–J · 697 Å² buried · 4 hydrogen bonds · protein-protein
D–I · 697 Å² buried · 4 hydrogen bonds · protein-protein
A–F · 696 Å² buried · 4 hydrogen bonds · protein-protein
B–G · 690 Å² buried · 4 hydrogen bonds · protein-protein
C–H · 668 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 covalent, 10 disulfide (covalent ligand, disulfide).

Compared structures

1SOS · Atomic structures of wild-type and thermostable mutant recombinant human cu, zn… · 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 1SOS · PDBe 1SOS · UniProt P00441

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