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Structure of L-amino acid deaminase from proteus myxofaciens in complex with anthranilate

Analyse Structure of L-amino acid deaminase from proteus myxofaciens in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FJN
Type: protein
Length: 894 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-amino acid deaminase
Ligands: FAD, BE2
Pockets: 5 · best druggability 0.83

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	L-amino acid deaminase	protein	447	32% helix, 24% strand	—

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
BE2 · 2-aminobenzoic acid · ligand · 2 copies · chains A, B

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

Pockets

5 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	863	0.83	0.85	89	FAD, BE2
2	845	0.82	0.85	91	FAD, BE2
3	1078	0.81	0.83	93	empty
4	242	0.74	0.88	37	empty
5	283	0.73	0.87	33	empty

Interfaces

1 interface between chains.

A–B · 800 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

5FJN · Structure of L-Amino acid deaminase from Proteus myxofaciens in complex with anthranilate · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 5FJN · PDBe 5FJN

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