› 3bpp

X-ray diffraction
2.3Å resolution

1510-N membrane protease K138A mutant specific for a stomatin homolog from Pyrococcus horikoshii

Released:
DOI: 10.2210/pdb3bpp/pdb
PDB entry 3bpp coloured by chain, front view.
PDB entry 3bpp coloured by chain, side view.
PDB entry 3bpp coloured by chain, top view.
Source organism: Pyrococcus horikoshii
Primary publication:
Novel dimer structure of a membrane-bound protease with a catalytic Ser-Lys dyad and its linkage to stomatin.
Yokoyama H, Hamamatsu S, Fujii S, Matsui I
J Synchrotron Radiat 15 254-7 (2008)
PMID: 18421152

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129821 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Membrane-bound protease PH1510 Chain: A
Molecule details ›
Chain: A
Length: 230 amino acids
Theoretical weight: 25.37 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
  • Canonical: O59179 (Residues: 16-236; Coverage: 51%)
Gene name: PH1510
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: I422
Unit cell:
a: 106.261Å b: 106.261Å c: 128.994Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.244 0.237 0.31
Expression system: Escherichia coli

Quick links

Citations

4 mentions without citation

PepPro: A Nonredundant Structure Data Set for Benchmarking Peptide-Protein Computational Docking.
Xu et al. (2020)
3 more