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Ancestral L-lys oxidase K387A variant (L-arg binding form)

Analyse Ancestral L-lys oxidase K387A variant (L-arg binding form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EIJ
Type: protein
Length: 1,172 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FAD dependent L-lys oxidase
Ligands: FAD, ARG
Pockets: 11 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	FAD dependent L-lys oxidase	protein	586	31% helix, 21% strand	—

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
ARG · Arginine · ligand · chains 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	798	0.87	0.90	106	FAD, ARG
2	963	0.87	0.88	117	FAD
3	821	0.81	0.84	79	empty
4	164	0.56	0.81	21	empty
5	110	0.51	0.81	18	empty

Interfaces

1 interface between chains.

A–B · 1831 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

7EIJ · Ancestral L-Lys oxidase K387A variant (L-Arg binding form) · the same entry in another collection · chain B against B, 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 7EIJ · PDBe 7EIJ

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