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Crystal structure of chbp, a cif homologue from burkholderia pseudomallei

Analyse Crystal structure of chbp, a cif homologue from burkholderia pseudomallei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3EIR
Type
protein
Length
491 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative ATP/GTP binding protein
UniProt
Q63KH5
Pockets
3 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative ATP/GTP binding proteinprotein24647% helix, 13% strandQ63KH5
BPutative ATP/GTP binding proteinprotein24548% helix, 13% strandQ63KH5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110580.850.86121empty
2500.290.7617empty
3510.290.7617empty

Interfaces

1 interface between chains.

  • A–B · 1387 Ų buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

  • 3EIR · Crystal structure of CHBP, a Cif Homologue from Burkholderia pseudomallei · the same entry in another collection · chain A against A, TM-score 1.00

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