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Monomeric human CU,ZN superoxide dismutase, loops IV and VII deleted, apo form, mutant H43F

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: 4BD4
Type: protein
Length: 941 residues
Chains: 9
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: 15 · best druggability 0.76

Structure

x-ray diffraction · 8 distinct chains · 0% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	109	0% helix, 50% strand	P00441
C	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	108	0% helix, 53% strand	P00441
D	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	104	0% helix, 52% strand	P00441
E	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	104	0% helix, 54% strand	P00441
F	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	102	0% helix, 51% strand	P00441
G	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	107	0% helix, 50% strand	P00441
H	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	100	0% helix, 52% strand	P00441
I	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	98	0% helix, 53% strand	P00441

Ligands and binding sites

GOL · Glycerol · additive · 4 copies · chains A, E, B, F, C, G, H

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

Pockets

15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	74	0.76	0.99	21	GOL
2	68	0.74	0.98	21	GOL
3	64	0.73	0.98	21	GOL
4	539	0.73	0.81	56	empty
5	450	0.69	0.80	37	empty

Interfaces

13 interfaces between chains.

C–G · 889 Å² buried · 23 hydrogen bonds · protein-protein
B–F · 854 Å² buried · 22 hydrogen bonds · protein-protein
A–E · 837 Å² buried · 18 hydrogen bonds · protein-protein
A–C · 438 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 428 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4BD4 · Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, 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 4BD4 · PDBe 4BD4 · UniProt P00441

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