MolNFT v1 · #57357 · protein

Crystal structure of pro- protein-glutaminase

3A56: “Crystal structure of pro- protein-glutaminase”. X-ray diffraction, 8 pockets (best druggability 0.72). MolNFT v1 #57357 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3A56
Type: protein
Length: 563 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein-glutaminase
EC: 3.5.1.-
UniProt: Q9AQQ8
Pockets: 8 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein-glutaminase (EC 3.5.1.-)	protein	282	25% helix, 34% strand	Q9AQQ8
B	Protein-glutaminase (EC 3.5.1.-)	protein	281	25% helix, 33% strand	Q9AQQ8

Ligands and binding sites

CIT · Citric acid · additive · 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, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	598	0.72	0.80	57	empty
2	253	0.68	0.84	35	empty
3	222	0.68	0.85	35	empty
4	508	0.67	0.78	51	empty
5	358	0.57	0.75	36	CIT

Interfaces

1 interface between chains.

A–B · 655 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

3A56 · Crystal structure of pro- protein-glutaminase · 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 Q9AQQ8
Elsewhere: RCSB PDB 3A56 · PDBe 3A56 · UniProt Q9AQQ8

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