MolNFT v1 · #100311 · protein

Ni- and zn-bound GLOA2 at high resolution

4MTS · Lactoylglutathione lyase: “Ni- and zn-bound GLOA2 at high resolution”. X-ray diffraction, 2 ligands (ZN, NI), 3 pockets (best druggability 0.57). MolNFT v1 #100311 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4MTS
Type: protein
Length: 256 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lactoylglutathione lyase
EC: 4.4.1.5
UniProt: Q9I5L8
Ligands: ZN, NI
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lactoylglutathione lyase (EC 4.4.1.5)	protein	129	16% helix, 45% strand	Q9I5L8
B	Lactoylglutathione lyase (EC 4.4.1.5)	protein	127	19% helix, 42% strand	Q9I5L8

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
NI · Nickel (II) ion · metal · chains A, B
GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

3 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	250	0.57	0.78	31	GOL
2	112	0.43	0.77	17	ZN
3	120	0.40	0.75	19	empty

Interfaces

1 interface between chains.

A–B · 2009 Å² buried · 38 hydrogen bonds · protein-protein

Compared structures

4MTS · Ni- and Zn-bound GloA2 at high resolution · 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 Q9I5L8
Elsewhere: RCSB PDB 4MTS · PDBe 4MTS · UniProt Q9I5L8

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