MolNFT v1 · #102514 · protein

The 1.55A crystal structure of NAF1 (MINER1): the redox-active 2FE-2S protein

4OO7 · Cdgsh iron-sulfur domain-containing protein 2: “The 1.55A crystal structure of NAF1 (MINER1): the redox-active 2FE-2S protein”. X-ray diffraction, 1 ligand (FES). MolNFT v1 #102514 on GenesisL1: 3D structure, binding sites and…

PDB: 4OO7
Type: protein
Length: 131 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	64	19% helix, 28% strand	Q8N5K1
B	Cdgsh iron-sulfur domain-containing protein 2	protein	67	18% helix, 27% 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 · 1778 Å² buried · 48 hydrogen bonds · protein-protein

Compared structures

4OO7 · THE 1.55A CRYSTAL STRUCTURE of NAF1 (MINER1): THE REDOX-ACTIVE 2FE-2S PROTEIN · 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 0.98

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 4OO7 · PDBe 4OO7 · UniProt Q8N5K1

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