MolNFT v1 · #178670 · protein

Universal stress protein (usp) domain of kdpd histidine kinase in complex with second messenger C-di-AMP

7JI4: “Universal stress protein (usp) domain of kdpd histidine kinase in complex with second messenger C-di-AMP”. X-ray diffraction, 1 ligand (2BA), 1 pocket (best druggability 0.72). MolNFT v1 #178670 on GenesisL1: 3D structure, binding…

PDB: 7JI4
Type: protein
Length: 125 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kdpd
UniProt: A0A167RS01
Ligands: 2BA
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kdpd	protein	125	38% helix, 24% strand	A0A167RS01

Ligands and binding sites

2BA · (2r,3r,3as,5r,7ar,9r,10r,10as,12r,14ar)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-D:3', 2'-J][1,3,7,9,2,8 ]tetraoxadiphosphacyclododecine-3,5, 10,12-tetrol 5,12-dioxide · ligand · 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	545	0.72	0.80	48	2BA

Compared structures

7JI4 · Universal stress protein (USP) domain of KdpD histidine kinase in complex with second… · 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 A0A167RS01
Elsewhere: RCSB PDB 7JI4 · PDBe 7JI4 · UniProt A0A167RS01

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