MolNFT v1 · #14218 · protein

Crystal structure at 1.5 ångströms resolution of the wild type thioredoxin-like [2FE-2S] ferredoxin from aquifex aeolicus

1M2A: “Crystal structure at 1.5 ångströms resolution of the wild type thioredoxin-like [2FE-2S] ferredoxin from…”. X-ray diffraction, 3 ligands (FES, ZN, SO4). MolNFT v1 #14218 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1M2A
Type: protein
Length: 204 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: [2FE-2S] ferredoxin
UniProt: O66511
Ligands: FES, ZN, SO4

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	[2FE-2S] ferredoxin	protein	103	34% helix, 21% strand	O66511
B	[2FE-2S] ferredoxin	protein	101	36% helix, 22% strand	O66511

Ligands and binding sites

FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, B
ZN · Zinc ion · metal · 4 copies · chains A
SO4 · Sulfate ion · ion · 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 · 526 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

1M2A · Crystal structure at 1.5 Angstroms resolution of the wild type thioredoxin-like [2Fe-2S]… · the same entry in another collection · chain A against A, TM-score 1.00
O66511 · AlphaFold monomer V2.0 prediction for ferredoxin, 2FE-2S (O66511) · 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 O66511
Elsewhere: RCSB PDB 1M2A · PDBe 1M2A · UniProt O66511

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