Research workbench

Crystal structure of adenylate kinase from aquifex aeolicus in complex with AP5A

Analyse Crystal structure of adenylate kinase from aquifex aeolicus in complex with AP5A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RGX
Type: protein
Length: 203 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenylate kinase
EC: 2.7.4.3
UniProt: O66490
Ligands: AP5, ZN
Pockets: 1 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenylate kinase (EC 2.7.4.3)	protein	203	53% helix, 16% strand	O66490

Ligands and binding sites

AP5 · Bis(adenosine)-5'-pentaphosphate · ligand · chains A
ZN · Zinc ion · metal · 4 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	648	0.81	0.85	76	ZN, AP5

Compared structures

2RGX · Crystal Structure of Adenylate Kinase from Aquifex Aeolicus in complex with Ap5A · the same entry in another collection · chain A against A, TM-score 1.00
O66490 · AlphaFold monomer V2.0 prediction for adenylate kinase (O66490) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 O66490
Elsewhere: RCSB PDB 2RGX · PDBe 2RGX · UniProt O66490

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