Research workbench

Structure of the N-terminal domain of escherichia COLI glutamine synthetase adenylyltransferase

Analyse Structure of the N-terminal domain of escherichia COLI glutamine synthetase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1V4A
Type: protein
Length: 429 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate-ammonia-ligase adenylyltransferase
EC: 2.7.7.42
UniProt: P30870
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamate-ammonia-ligase adenylyltransferase (EC 2.7.7.42)	protein	429	63% helix, 6% strand	P30870

Pockets

4 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	402	0.63	0.78	43	empty
2	55	0.48	0.85	14	empty
3	64	0.32	0.76	16	empty
4	56	0.29	0.75	16	empty

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

1V4A · Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase… · the same entry in another collection · chain A against A, TM-score 1.00
P30870 · AlphaFold monomer V2.0 prediction for bifunctional glutamine synthetase… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P30870
Elsewhere: RCSB PDB 1V4A · PDBe 1V4A · UniProt P30870

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