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Crystal structure of apo-H46R familial als mutant human CU,ZN superoxide dismutase (cuznsod) to 2.5A resolution

Analyse Crystal structure of apo-H46R familial als mutant human CU,ZN superoxide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OZT
Type: protein
Length: 1,097 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Superoxide dismutase [cu-zn]
EC: 1.15.1.1
UniProt: P00441
Pockets: 10 · best druggability 0.64

Structure

x-ray diffraction · 7 distinct chains · 7% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
M, N	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	153	9% helix, 41% strand	P00441
G	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	130	6% helix, 48% strand	P00441
H	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	135	6% helix, 46% strand	P00441
K	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	126	6% helix, 49% strand	P00441
L	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	130	6% helix, 48% strand	P00441
I	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	135	6% helix, 46% strand	P00441
J	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	135	6% helix, 46% strand	P00441

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	227	0.64	0.83	36	empty
2	195	0.63	0.84	34	empty
3	256	0.63	0.81	33	empty
4	430	0.62	0.77	54	empty
5	178	0.62	0.84	30	empty

Interfaces

7 interfaces between chains.

K–L · 727 Å² buried · 4 hydrogen bonds · protein-protein
M–N · 717 Å² buried · 4 hydrogen bonds · protein-protein
G–H · 712 Å² buried · 4 hydrogen bonds · protein-protein
I–J · 705 Å² buried · 4 hydrogen bonds · protein-protein
K–J · 307 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

1OZT · Crystal Structure of apo-H46R Familial ALS Mutant human Cu,Zn Superoxide Dismutase… · the same entry in another collection · chain M against M, 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 1OZT · PDBe 1OZT · UniProt P00441

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