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Crystal structure of pure (BA0288) from bacillus anthracis at 1.8 resolution

Analyse Crystal structure of pure (BA0288) from bacillus anthracis at 1.8 resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1XMP
Type
protein
Length
1,270 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phosphoribosylaminoimidazole carboxylase
EC
4.1.1.21
UniProt
Q81ZH8
Pockets
16 · best druggability 0.85

Structure

x-ray diffraction · 4 distinct chains · 48% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, D, EPhosphoribosylaminoimidazole carboxylase (EC 4.1.1.21)protein15548% helix, 16% strandQ81ZH8
BPhosphoribosylaminoimidazole carboxylase (EC 4.1.1.21)protein15748% helix, 15% strandQ81ZH8
C, GPhosphoribosylaminoimidazole carboxylase (EC 4.1.1.21)protein16448% helix, 14% strandQ81ZH8
F, HPhosphoribosylaminoimidazole carboxylase (EC 4.1.1.21)protein16048% helix, 14% strandQ81ZH8

Pockets

16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16390.850.8942empty
24490.650.7860empty
33450.640.7934empty
43460.610.7838empty
53110.610.7833empty

Interfaces

16 interfaces between chains.

  • C–D · 1886 Ų buried · 36 hydrogen bonds · protein-protein
  • G–H · 1870 Ų buried · 33 hydrogen bonds · protein-protein
  • E–F · 1844 Ų buried · 38 hydrogen bonds · protein-protein
  • A–B · 1772 Ų buried · 35 hydrogen bonds · protein-protein
  • B–C · 1003 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 1XMP · Crystal Structure of PurE (BA0288) from Bacillus anthracis at 1.8 Resolution · the same entry in another collection · chain A against A, TM-score 1.00

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