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Crystal structure of H.PYLORI phosphopantetheine adenylyltransferase mutant I4V/N76Y

Analyse Crystal structure of H.PYLORI phosphopantetheine adenylyltransferase mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NV7
Type: protein
Length: 155 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphopantetheine adenylyltransferase
EC: 2.7.7.3
UniProt: O26010
Ligands: SO4
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphopantetheine adenylyltransferase (EC 2.7.7.3)	protein	155	41% helix, 13% strand	O26010

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A
ACY · Acetic acid · additive · 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	283	0.56	0.77	36	ACY

Compared structures

3NV7 · Crystal structure of H.pylori phosphopantetheine adenylyltransferase mutant I4V/N76Y · the same entry in another collection · chain A against A, TM-score 1.00
O26010 · AlphaFold monomer V2.0 prediction for phosphopantetheine adenylyltransferase (O26010) · a predicted model of the same protein · chain A against A, TM-score 0.58

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 O26010
Elsewhere: RCSB PDB 3NV7 · PDBe 3NV7 · UniProt O26010

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