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Crystal structure of burkholderia xenovorans dmrb in complex with FMN: a cubic protein cage for redox transfer

Analyse Crystal structure of burkholderia xenovorans dmrb in complex with FMN: a cubic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WIS
Type: protein
Length: 180 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative dihydromethanopterin reductase (afpa)
UniProt: Q13QT8
Ligands: FMN, SO4
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative dihydromethanopterin reductase (afpa)	protein	180	43% helix, 23% strand	Q13QT8

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 2 copies · chains A
SO4 · Sulfate ion · ion · 4 copies · 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	73	0.31	0.74	17	empty

Compared structures

3WIS · Crystal structure of Burkholderia xenovorans DmrB in complex with FMN: A Cubic Protein… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt Q13QT8
Elsewhere: RCSB PDB 3WIS · PDBe 3WIS · UniProt Q13QT8

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