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Crystal structure of zymomonas mobilis glutaminyl cyclase (monoclinic form)

Analyse Crystal structure of zymomonas mobilis glutaminyl cyclase (monoclinic form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NOM
Type: protein
Length: 468 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamine cyclotransferase
EC: 2.3.2.5
UniProt: C5TI01
Ligands: CA, SO4
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutamine cyclotransferase (EC 2.3.2.5)	protein	234	2% helix, 56% strand	C5TI01

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A, B
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	746	0.76	0.80	76	SO4
2	202	0.48	0.75	26	empty
3	56	0.37	0.80	16	empty

Interfaces

1 interface between chains.

A–B · 567 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

3NOM · Crystal Structure of Zymomonas mobilis Glutaminyl Cyclase (monoclinic form) · 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 C5TI01
Elsewhere: RCSB PDB 3NOM · PDBe 3NOM · UniProt C5TI01

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