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Crystal structure of MINER1: the redox-active 2FE-2S protein causative in wolfram syndrome 2

Analyse Crystal structure of MINER1: the redox-active 2FE-2S protein causative in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FNV
Type: protein
Length: 135 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cdgsh iron sulfur domain-containing protein 2
UniProt: Q8N5K1
Ligands: FES

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cdgsh iron sulfur domain-containing protein 2	protein	67	18% helix, 27% strand	Q8N5K1
B	Cdgsh iron sulfur domain-containing protein 2	protein	68	18% helix, 26% strand	Q8N5K1

Ligands and binding sites

FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, B

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

Interfaces

1 interface between chains.

A–B · 1784 Å² buried · 45 hydrogen bonds · protein-protein

Compared structures

3FNV · Crystal Structure of Miner1: The Redox-active 2Fe-2S Protein Causative in Wolfram… · the same entry in another collection · chain A against A, TM-score 1.00
Q8N5K1 · AlphaFold monomer V2.0 prediction for cdgsh iron-sulfur domain- containing protein 2… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q8N5K1
Elsewhere: RCSB PDB 3FNV · PDBe 3FNV · UniProt Q8N5K1

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