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Crystal structure of edds lyase in complex with ss-edds

Analyse Crystal structure of edds lyase in complex with ss-edds in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6G3H
Type: protein
Length: 497 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Argininosuccinate lyase
UniProt: Q11KV9
Ligands: EKQ
Pockets: 5 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 68% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Argininosuccinate lyase	protein	497	68% helix, 4% strand	Q11KV9

Ligands and binding sites

EKQ · (2~{S})-2-[2-[[(2~{S})-1,4-bis(oxidanyl)-1,4-bis(oxidanylidene)butan-2-yl]amino]ethylamino]butanedioic acid · ligand · chains A

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	130	0.47	0.78	23	empty
2	58	0.43	0.82	16	empty
3	80	0.35	0.76	16	empty
4	63	0.34	0.77	16	empty
5	57	0.26	0.73	14	empty

Compared structures

6G3H · Crystal structure of EDDS lyase in complex with SS-EDDS · 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 6G3H · PDBe 6G3H · UniProt Q11KV9

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