MolNFT v1 · #149539 · protein

Crystal structure of edds lyase in complex with N-(2-aminoethyl) aspartic acid (aeaa)

6G3I · Argininosuccinate lyase: “Crystal structure of edds lyase in complex with N-(2-aminoethyl) aspartic acid (aeaa)”. X-ray diffraction, 2 ligands (EKN, FUM), 6 pockets (best druggability 0.50). MolNFT v1 #149539 on GenesisL1: 3D…

PDB: 6G3I
Type: protein
Length: 496 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Argininosuccinate lyase
UniProt: Q11KV9
Ligands: EKN, FUM
Pockets: 6 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Argininosuccinate lyase	protein	496	69% helix, 4% strand	Q11KV9

Ligands and binding sites

EKN · (2~{S})-2-(2-azanylethylamino)butanedioic acid · ligand · chains A
FUM · Fumaric acid · ligand · chains A

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

Pockets

6 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	142	0.50	0.79	23	empty
2	59	0.39	0.80	16	empty
3	71	0.33	0.76	16	empty
4	56	0.33	0.77	15	empty
5	72	0.32	0.74	12	empty

Compared structures

6G3I · Crystal structure of EDDS lyase in complex with N-(2-aminoethyl)aspartic acid (AEAA) · 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 Q11KV9
Elsewhere: RCSB PDB 6G3I · PDBe 6G3I · UniProt Q11KV9

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