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Leptolyngbya boryana ferredoxin

Analyse Leptolyngbya boryana ferredoxin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3B2G
Type: protein
Length: 196 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferredoxin-1
UniProt: Q51577
Ligands: FES

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ferredoxin-1	protein	98	22% helix, 35% strand	Q51577

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 · 425 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

3B2G · Leptolyngbya boryana Ferredoxin · the same entry in another collection · chain A against A, TM-score 1.00
Q51577 · AlphaFold monomer V2.0 prediction for ferredoxin-1 (Q51577) · a predicted model of the same protein · chain A 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 Q51577
Elsewhere: RCSB PDB 3B2G · PDBe 3B2G · UniProt Q51577

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