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Crystal structure of PPK2 class III in the complex with AMP from cytophaga hutchinsonii atcc 33406

Analyse Crystal structure of PPK2 class III in the complex with AMP from cytophaga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ANG
Type: protein
Length: 297 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: POLYPHOSPHATE:AMP phosphotransferase
EC: 2.7.4.-
UniProt: Q11YW6
Ligands: AMP, CL
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	POLYPHOSPHATE:AMP phosphotransferase (EC 2.7.4.-)	protein	297	54% helix, 11% strand	Q11YW6

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · chains A
CL · Chloride ion · ion · chains A

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

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	208	0.63	0.83	33	AMP
2	71	0.48	0.83	16	CL
3	105	0.36	0.74	22	empty
4	52	0.28	0.75	16	empty

Compared structures

6ANG · Crystal structure of PPK2 Class III in the complex with AMP from Cytophaga hutchinsonii… · 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 Q11YW6
Elsewhere: RCSB PDB 6ANG · PDBe 6ANG · UniProt Q11YW6

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