Research workbench

Clostridium beijerinckii flavodoxin mutant: G57T reduced (277K)

Analyse Clostridium beijerinckii flavodoxin mutant: G57T reduced (277K) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FVX
Type: protein
Length: 138 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flavodoxin
UniProt: P00322
Ligands: FMN
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flavodoxin	protein	138	41% helix, 22% strand	P00322

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.35	0.76	23	FMN

Compared structures

2FVX · Clostridium beijerinckii flavodoxin mutant: G57T reduced (277K) · the same entry in another collection · chain A against A, TM-score 1.00
P00322 · AlphaFold monomer V2.0 prediction for flavodoxin (P00322) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 P00322
Elsewhere: RCSB PDB 2FVX · PDBe 2FVX · UniProt P00322

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