MolNFT v1 · #88213 · protein

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

4CNZ · Pii-like protein pz: “Structure of pii signaling protein glnz from azospirillum brasilense in complex with adenosine diphosphate”. X-ray diffraction, 1 ligand (ADP), 11 pockets (best druggability 0.80). MolNFT v1 #88213 on…

PDB: 4CNZ
Type: protein
Length: 615 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pii-like protein pz
UniProt: P70731
Ligands: ADP
Pockets: 11 · best druggability 0.80

Structure

x-ray diffraction · 4 distinct chains · 29% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D	Pii-like protein pz	protein	100	29% helix, 37% strand	P70731
C	Pii-like protein pz	protein	101	29% helix, 38% strand	P70731
E	Pii-like protein pz	protein	112	30% helix, 33% strand	P70731
F	Pii-like protein pz	protein	102	28% helix, 37% strand	P70731

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A, C, B, D, F, E

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

Pockets

11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	132	0.80	0.98	24	empty
2	182	0.77	0.93	33	ADP
3	183	0.76	0.92	34	ADP
4	181	0.75	0.91	35	ADP
5	195	0.74	0.90	34	ADP

Interfaces

12 interfaces between chains.

D–E · 1144 Å² buried · 21 hydrogen bonds · protein-protein
E–F · 1119 Å² buried · 18 hydrogen bonds · protein-protein
B–C · 1119 Å² buried · 18 hydrogen bonds · protein-protein
D–F · 1093 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 1057 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

4CNZ · 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 4CNZ · PDBe 4CNZ · UniProt P70731

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