› 3unx

X-ray diffraction
1.26Å resolution

Bond length analysis of asp, glu and his residues in subtilisin Carlsberg at 1.26A resolution

Released:
DOI: 10.2210/pdb3unx/pdb
PDB entry 3unx coloured by chain, front view.
PDB entry 3unx coloured by chain, side view.
PDB entry 3unx coloured by chain, top view.
Source organism: Bacillus licheniformis
Primary publication:
Protonation-state determination in proteins using high-resolution X-ray crystallography: effects of resolution and completeness.
Fisher SJ, Blakeley MP, Cianci M, McSweeney S, Helliwell JR
Acta Crystallogr D Biol Crystallogr 68 800-9 (2012)
PMID: 22751665

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133525 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin Carlsberg Chain: A
Molecule details ›
Chain: A
Length: 274 amino acids
Theoretical weight: 27.28 KDa
Source organism: Bacillus licheniformis
Expression system: Escherichia coli
UniProt:
  • Canonical: P00780 (Residues: 106-379; Coverage: 78%)
Gene names: apr, subC
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

3 bound ligands:
Ligand GOL 4 x GOL
Ligand CA 2 x CA
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P212121
Unit cell:
a: 52.099Å b: 55.159Å c: 75.453Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.119 0.118 0.139
Expression system: Escherichia coli

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Citations

1 review citation

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Houben et al. (2014)
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4 mentions without citation

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Dahms et al. (2016)
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