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Crystal structure analysis of mglu in its glutamate form

Analyse Crystal structure analysis of mglu in its glutamate form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IHA
Type: protein
Length: 873 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Salt-tolerant glutaminase
EC: 3.5.1.2
UniProt: Q4U1A6
Ligands: GLU
Pockets: 8 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Salt-tolerant glutaminase (EC 3.5.1.2)	protein	435	46% helix, 16% strand	Q4U1A6
B	Salt-tolerant glutaminase (EC 3.5.1.2)	protein	438	46% helix, 16% strand	Q4U1A6

Ligands and binding sites

GLU · Glutamic acid · ligand · 2 copies · chains A, B

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

Pockets

8 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	402	0.63	0.78	32	GLU
2	346	0.60	0.77	45	GLU
3	231	0.46	0.73	35	empty
4	100	0.33	0.73	22	empty
5	72	0.32	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 727 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

3IHA · Crystal Structure Analysis of Mglu in its glutamate 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 Q4U1A6
Elsewhere: RCSB PDB 3IHA · PDBe 3IHA · UniProt Q4U1A6

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