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Monomeric human CU,ZN superoxide dismutase, loops IV and VII deleted, apo form.

Analyse Monomeric human CU,ZN superoxide dismutase, loops IV and VII deleted, apo form. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BCZ
Type: protein
Length: 219 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
Pockets: 3 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	110	0% helix, 54% strand	P00441
B	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	109	0% helix, 53% strand	P00441

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	88	0.38	0.77	17	empty
2	133	0.37	0.73	17	empty
3	82	0.36	0.76	21	empty

Interfaces

1 interface between chains.

A–B · 479 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

4BCZ · Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form. · 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 4BCZ · PDBe 4BCZ · UniProt P00441

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