Research workbench

Crystal structure of gamma-glutamyl hydrolase (C108A) from zebrafish

Analyse Crystal structure of gamma-glutamyl hydrolase (C108A) from zebrafish in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4L8Y
Type: protein
Length: 1,148 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gamma-glutamyl hydrolase
EC: 3.4.19.9
UniProt: Q6NY42
Pockets: 12 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, D, A, B	Gamma-glutamyl hydrolase (EC 3.4.19.9)	protein	287	36% helix, 27% strand	Q6NY42

Pockets

12 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	72	0.75	0.98	21	empty
2	75	0.74	0.98	24	empty
3	775	0.74	0.79	86	empty
4	521	0.69	0.79	46	empty
5	163	0.47	0.76	38	empty

Interfaces

3 interfaces between chains.

A–B · 1735 Å² buried · 11 hydrogen bonds · protein-protein
C–D · 1693 Å² buried · 13 hydrogen bonds · protein-protein
D–A · 734 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

4L8Y · Crystal structure of gamma-glutamyl hydrolase (C108A) from zebrafish · the same entry in another collection · chain C against C, 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 Q6NY42
Elsewhere: RCSB PDB 4L8Y · PDBe 4L8Y · UniProt Q6NY42

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