MolNFT v1 · #153110 · protein

Crystal structure of the complex of phosphopantetheine adenylyltransferase from acinetobacter baumannii with pyrophosphate at 2.30A resolution

6J3M: “Crystal structure of the complex of phosphopantetheine adenylyltransferase from acinetobacter baumannii with…”. X-ray diffraction, 3 ligands (POP, CL, SO4), 1 pocket (best druggability 0.62). MolNFT v1 #153110 on GenesisL1: 3D…

PDB: 6J3M
Type: protein
Length: 163 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphopantetheine adenylyltransferase
EC: 2.7.7.3
UniProt: A0A059ZFC5
Ligands: POP, CL, SO4
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphopantetheine adenylyltransferase (EC 2.7.7.3)	protein	163	44% helix, 17% strand	A0A059ZFC5

Ligands and binding sites

POP · Pyrophosphate 2- · ligand · chains A
CL · Chloride ion · ion · 2 copies · chains A
SO4 · Sulfate ion · ion · 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	331	0.62	0.78	40	POP, CL

Compared structures

6J3M · Crystal structure of the complex of Phosphopantetheine adenylyltransferase from… · 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 A0A059ZFC5
Elsewhere: RCSB PDB 6J3M · PDBe 6J3M · UniProt A0A059ZFC5

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