MolNFT v1 · #121703 · protein

High resolution structure of L-amino acid deaminase from proteus vulgaris with the deletion of the specific insertion sequence

5I39: “High resolution structure of L-amino acid deaminase from proteus vulgaris with the deletion of the specific…”. X-ray diffraction, 1 ligand (FAD), 2 pockets (best druggability 0.80). MolNFT v1 #121703 on GenesisL1: 3D structure…

PDB: 5I39
Type: protein
Length: 383 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-amino acid deaminase
UniProt: Q9LCB2
Ligands: FAD
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-amino acid deaminase	protein	383	30% helix, 24% strand	Q9LCB2

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
EDO · 1,2-ethanediol · additive · 9 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	551	0.80	0.86	83	FAD, EDO
2	58	0.39	0.80	13	empty

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

5I39 · High resolution structure of L-amino acid deaminase from Proteus vulgaris with the… · 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
Every structure of UniProt Q9LCB2
Elsewhere: RCSB PDB 5I39 · PDBe 5I39 · UniProt Q9LCB2

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