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Ancestral L-lys oxidase (ligand free form)

Analyse Ancestral L-lys oxidase (ligand free form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EIH
Type: protein
Length: 1,174 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FAD dependent enzyme
Ligands: FAD, SO4
Pockets: 15 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FAD dependent enzyme	protein	588	31% helix, 20% strand	—
B	FAD dependent enzyme	protein	586	32% helix, 20% strand	—

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1159	0.86	0.87	122	SO4, FAD
2	1196	0.82	0.83	130	FAD
3	133	0.80	0.98	35	empty
4	800	0.75	0.79	64	empty
5	51	0.67	0.97	21	empty

Interfaces

1 interface between chains.

A–B · 1890 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

7EIH · Ancestral L-Lys oxidase (ligand free form) · 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 7EIH · PDBe 7EIH

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