Research workbench

W288A mutant of glxa from streptomyces lividans: cu-bound form

Analyse W288A mutant of glxa from streptomyces lividans: cu-bound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LXZ
Type: protein
Length: 601 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Secreted protein
UniProt: D6EWM0
Ligands: CU, PO4
Pockets: 5 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Secreted protein	protein	601	6% helix, 40% strand	D6EWM0

Ligands and binding sites

CU · Copper (II) ion · metal · 2 copies · chains B
PO4 · Phosphate ion · ion · 2 copies · chains B
EDO · 1,2-ethanediol · additive · 10 copies · chains B
ACT · Acetate ion · additive · 2 copies · chains 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	134	0.77	0.95	26	empty
2	82	0.73	0.96	24	empty
3	197	0.50	0.76	26	EDO
4	88	0.34	0.74	22	EDO
5	59	0.30	0.75	17	empty

Compared structures

5LXZ · W288A mutant of GlxA from Streptomyces lividans: Cu-bound 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
Every structure of UniProt D6EWM0
Elsewhere: RCSB PDB 5LXZ · PDBe 5LXZ · UniProt D6EWM0

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