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Crystal structure of a putative serine hydrolase (XCC3885) from xanthomonas campestris pv. campestris at 2.69 a resolution

Analyse Crystal structure of a putative serine hydrolase (XCC3885) from xanthomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3KSR
Type
protein
Length
243 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative serine hydrolase
UniProt
Q8P431
Ligands
PO4, CL

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative serine hydrolaseprotein24337% helix, 26% strandQ8P431

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 2 copies · chains A
  • CL · Chloride ion · ion · chains A

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

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

  • 3KSR · Crystal structure of a putative serine hydrolase (XCC3885) from xanthomonas campestris… · the same entry in another collection · chain A against A, TM-score 1.00

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