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The complex of pii and pipx from anabaena

Analyse The complex of pii and pipx from anabaena in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3N5B
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nitrogen regulatory protein P-II; ASR0485 protein
UniProt: Q9L422, Q8YZH5
Ligands: ADP, SO4
Pockets: 4 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nitrogen regulatory protein P-II	protein	112	29% helix, 32% strand	Q9L422
B	ASR0485 protein	protein	86	37% helix, 34% strand	Q8YZH5

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	344	0.56	0.75	35	empty
2	209	0.52	0.77	22	empty
3	74	0.52	0.85	19	SO4
4	90	0.38	0.76	17	ADP

Interfaces

1 interface between chains.

A–B · 622 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3N5B · The complex of PII and PipX from Anabaena · 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 Q9L422
Every structure of UniProt Q8YZH5
Elsewhere: RCSB PDB 3N5B · PDBe 3N5B · UniProt Q9L422 · UniProt Q8YZH5

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