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Crystal structure of FMN-bound protein MM1853 from methanosarcina mazei, pfam DUF447

Analyse Crystal structure of FMN-bound protein MM1853 from methanosarcina mazei, pfam… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2NR4
Type
protein
Length
373 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Conserved hypothetical protein
UniProt
Q8PVV4
Ligands
FMN
Pockets
4 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AConserved hypothetical proteinprotein19140% helix, 32% strandQ8PVV4
BConserved hypothetical proteinprotein18238% helix, 35% strandQ8PVV4

Ligands and binding sites

  • FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15050.750.8351empty
23380.650.8031FMN
34290.620.7738FMN
4740.290.7219empty

Interfaces

1 interface between chains.

  • A–B · 1662 Ų buried · 32 hydrogen bonds · protein-protein

Compared structures

  • 2NR4 · Crystal structure of FMN-bound protein MM1853 from Methanosarcina mazei, Pfam DUF447 · the same entry in another collection · chain A against A, TM-score 1.00

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