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Crystal structure of the aldehyde oxidoreductase from desulfovibrio desulfuricans atcc 27774

Analyse Crystal structure of the aldehyde oxidoreductase from desulfovibrio… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1DGJ
Type: protein
Length: 906 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldehyde oxidoreductase
EC: 1.2.-.-
UniProt: Q9REC4
Ligands: FES, 2MO, MCN
Pockets: 8 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aldehyde oxidoreductase (EC 1.2.-.-)	protein	906	32% helix, 24% strand	Q9REC4

Ligands and binding sites

FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A
2MO · Molybdenum (iv)oxide · ligand · chains A
MCN · Pterin cytosine dinucleotide · ligand · chains A

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

Pockets

8 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	255	0.84	0.96	49	2MO, MCN
2	259	0.60	0.79	36	empty
3	171	0.48	0.77	25	empty
4	188	0.47	0.75	32	empty
5	95	0.39	0.77	23	empty

Compared structures

1DGJ · Crystal structure of the aldehyde oxidoreductase from desulfovibrio desulfuricans atcc… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt Q9REC4
Elsewhere: RCSB PDB 1DGJ · PDBe 1DGJ · UniProt Q9REC4

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