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Crystal structure of peptide deformylase from ehrlichia chaffeensis

Analyse Crystal structure of peptide deformylase from ehrlichia chaffeensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OCA
Type
protein
Length
358 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptide deformylase
EC
3.5.1.88
UniProt
Q2GI30
Ligands
ZN, CL
Pockets
3 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptide deformylase (EC 3.5.1.88)protein17932% helix, 28% strandQ2GI30
BPeptide deformylase (EC 3.5.1.88)protein17933% helix, 28% strandQ2GI30

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • CL · Chloride ion · ion · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18890.790.8192CL
21430.550.8119empty
31260.520.8122empty

Interfaces

1 interface between chains.

  • A–B · 610 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 3OCA · Crystal structure of peptide deformylase from Ehrlichia chaffeensis · the same entry in another collection · chain A against A, TM-score 1.00

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