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Human gamma-glutamylamine cyclotransferase complex with 5- oxoproline

Analyse Human gamma-glutamylamine cyclotransferase complex with 5- oxoproline in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3JUC
Type: protein
Length: 149 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AIG2-like domain-containing protein 1
EC: 2.3.2.4
UniProt: Q9BVM4
Ligands: PCA, NO3
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	AIG2-like domain-containing protein 1 (EC 2.3.2.4)	protein	149	15% helix, 34% strand	Q9BVM4

Ligands and binding sites

PCA · Pyroglutamic acid · ligand · chains A
NO3 · Nitrate ion · ion · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	88	0.59	0.87	21	PCA

Compared structures

3JUC · Human gamma-glutamylamine cyclotransferase complex with 5-oxoproline · the same entry in another collection · chain A against A, TM-score 1.00
Q9BVM4 · AlphaFold monomer V2.0 prediction for gamma- glutamylaminecyclotransferase (Q9BVM4) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9BVM4
Elsewhere: RCSB PDB 3JUC · PDBe 3JUC · UniProt Q9BVM4

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