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The 1.5 a resolution crystal structure of [FE3S4]- ferredoxin from the hyperthermophilic archaeon pyrococcus furiosus

Analyse The 1.5 a resolution crystal structure of [FE3S4]- ferredoxin from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SJ1
Type: protein
Length: 132 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferredoxin
UniProt: P29603
Ligands: NCO, F3S

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ferredoxin	protein	66	27% helix, 26% strand	P29603

Ligands and binding sites

NCO · Cobalt hexammine(iii) · ligand · 4 copies · chains A, B
F3S · FE3-S4 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 · 424 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1SJ1 · The 1.5 A Resolution Crystal Structure of [Fe3S4]-Ferredoxin from the hyperthermophilic… · the same entry in another collection · chain A against A, TM-score 1.00
P29603 · AlphaFold monomer V2.0 prediction for ferredoxin (P29603) · a predicted model of the same protein · chain B 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 P29603
Elsewhere: RCSB PDB 1SJ1 · PDBe 1SJ1 · UniProt P29603

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