Research workbench

Structure of pii signaling protein glnz from azospirillum brasilense in complex with adenosine diphosphate

Analyse Structure of pii signaling protein glnz from azospirillum brasilense in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4CO2
Type: protein
Length: 224 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pii-like protein pz
UniProt: P70731
Ligands: ADP
Pockets: 3 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pii-like protein pz	protein	112	29% helix, 36% strand	P70731

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
PG4 · Tetraethylene glycol · additive · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.32	0.76	13	ADP
2	54	0.29	0.75	13	ADP
3	54	0.27	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 48 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4CO2 · Structure of PII signaling protein GlnZ from Azospirillum brasilense in complex with… · 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 P70731
Elsewhere: RCSB PDB 4CO2 · PDBe 4CO2 · UniProt P70731

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