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Crystal structure of nisod H1A mutant

Analyse Crystal structure of nisod H1A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NCQ
Type: protein
Length: 330 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Superoxide dismutase [ni]
EC: 1.15.1.1
UniProt: P80735
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Superoxide dismutase [ni] (EC 1.15.1.1)	protein	112	79% helix, 0% strand	P80735
B, C	Superoxide dismutase [ni] (EC 1.15.1.1)	protein	109	83% helix, 0% strand	P80735

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	83	0.38	0.77	23	empty

Interfaces

3 interfaces between chains.

A–C · 340 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 338 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 331 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4NCQ · Crystal structure of NiSOD H1A mutant · the same entry in another collection · chain A against A, TM-score 1.00
P80735 · AlphaFold monomer V2.0 prediction for superoxide dismutase [ni] (P80735) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P80735
Elsewhere: RCSB PDB 4NCQ · PDBe 4NCQ · UniProt P80735

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