Research workbench

Crystal structure of chaetomium thermophilum glycerol kinase in P2221 space group

Analyse Crystal structure of chaetomium thermophilum glycerol kinase in P2221 space… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ZQ5
Type: protein
Length: 1,020 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycerol kinase-like protein
UniProt: G0SAG9
Pockets: 9 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glycerol kinase-like protein	protein	510	38% helix, 22% strand	G0SAG9

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 8 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1166	0.74	0.77	93	EDO
2	576	0.70	0.79	56	EDO
3	586	0.67	0.77	61	EDO
4	161	0.52	0.79	28	empty
5	166	0.48	0.77	25	empty

Interfaces

1 interface between chains.

A–B · 451 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

6ZQ5 · Crystal structure of Chaetomium thermophilum Glycerol Kinase in P2221 space group · 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 G0SAG9
Elsewhere: RCSB PDB 6ZQ5 · PDBe 6ZQ5 · UniProt G0SAG9

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.