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Apo-form of NAD-dependent formate dehydrogenase from bacterium moraxella SP.C-1 in closed conformation

Analyse Apo-form of NAD-dependent formate dehydrogenase from bacterium moraxella SP.C-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FN4
Type: protein
Length: 399 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD-dependent formate dehydrogenase
EC: 1.2.1.2
UniProt: O08375
Ligands: SO4
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NAD-dependent formate dehydrogenase (EC 1.2.1.2)	protein	399	35% helix, 17% strand	O08375

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	365	0.72	0.84	47	GOL, SO4
2	214	0.54	0.77	22	empty
3	94	0.43	0.78	20	empty
4	79	0.34	0.74	13	empty

Compared structures

3FN4 · Apo-form of NAD-dependent formate dehydrogenase from bacterium Moraxella sp.C-1 in closed… · the same entry in another collection · 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 O08375
Elsewhere: RCSB PDB 3FN4 · PDBe 3FN4 · UniProt O08375

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