MolNFT v1 · #122794 · protein

Monomeric human CU,ZN superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P1/2

5J07 · Superoxide dismutase [cu-ZN],SUPEROXIDE dismutase [cu-zn]…: “Monomeric human CU,ZN superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P1/2”. X-ray diffraction, 2 pockets (best druggability 0.41). MolNFT v1…

PDB: 5J07
Type: protein
Length: 230 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Superoxide dismutase [cu-ZN],SUPEROXIDE dismutase [cu-zn], superoxide dismutase…
EC: 1.15.1.1
UniProt: P00441
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Superoxide dismutase [cu-ZN],SUPEROXIDE dismutase [cu-zn], superoxide dismutase [cu-ZN],SUPEROXIDE dismutase [cu-zn] (EC 1.15.1.1)	protein	115	0% helix, 55% strand	P00441

Pockets

2 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	110	0.41	0.76	19	empty
2	108	0.40	0.76	23	empty

Interfaces

1 interface between chains.

A–B · 462 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

5J07 · Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular… · 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 5J07 · PDBe 5J07 · UniProt P00441

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