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Crystal structure of a phosphotransacetylase from streptococcus pyogenes

Analyse Crystal structure of a phosphotransacetylase from streptococcus pyogenes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1R5J
Type
protein
Length
658 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative phosphotransacetylase
EC
2.3.1.8
UniProt
Q99ZQ5
Pockets
4 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPutative phosphotransacetylase (EC 2.3.1.8)protein32945% helix, 16% strandQ99ZQ5

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14720.660.7850empty
24640.660.7846empty
31110.540.8323empty
41120.530.8326empty

Interfaces

1 interface between chains.

  • A–B · 1579 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified (engineered).

Compared structures

  • 1R5J · Crystal Structure of a Phosphotransacetylase from Streptococcus pyogenes · the same entry in another collection · chain A against A, TM-score 1.00

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