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Crystal structure of otemo (FAD bound form 2)

Analyse Crystal structure of otemo (FAD bound form 2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3UOX
Type: protein
Length: 1,070 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Otemo
EC: 1.-.-.-
Ligands: FAD
Pockets: 11 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Otemo (EC 1.-.-.-)	protein	537	37% helix, 21% strand	—
B	Otemo (EC 1.-.-.-)	protein	533	38% helix, 21% strand	—

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1130	0.85	0.85	116	empty
2	1007	0.84	0.85	90	FAD
3	1071	0.82	0.83	94	FAD
4	131	0.64	0.87	29	empty
5	283	0.52	0.74	37	empty

Interfaces

1 interface between chains.

A–B · 1119 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3UOX · Crystal Structure of OTEMO (FAD bound form 2) · 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
Elsewhere: RCSB PDB 3UOX · PDBe 3UOX

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