› 1kap

X-ray diffraction
1.64Å resolution

THREE-DIMENSIONAL STRUCTURE OF THE ALKALINE PROTEASE OF PSEUDOMONAS AERUGINOSA: A TWO-DOMAIN PROTEIN WITH A CALCIUM BINDING PARALLEL BETA ROLL MOTIF

Released:
DOI: 10.2210/pdb1kap/pdb
PDB entry 1kap coloured by chain, front view.
PDB entry 1kap coloured by chain, side view.
PDB entry 1kap coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif.
Baumann U, Wu S, Flaherty KM, McKay DB
EMBO J 12 3357-64 (1993)
PMID: 8253063

Function and Biology Details

Reaction catalysed: 
Preferential cleavage of bonds with hydrophobic residues in P1'.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162276 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serralysin Chain: P
Molecule details ›
Chain: P
Length: 479 amino acids
Theoretical weight: 50.46 KDa
Source organism: Pseudomonas aeruginosa PAO1
UniProt:
  • Canonical: Q03023 (Residues: 1-479; Coverage: 100%)
Gene names: PA1249, aprA
Sequence domains:
Structure domains:
TETRAPEPTIDE (GLY SER ASN SER) Chain: I
Molecule details ›
Chain: I
Length: 4 amino acids
Theoretical weight: 363 Da
Source organism: Pseudomonas aeruginosa PAO1

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand CA 8 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P65
Unit cell:
a: 106.9Å b: 106.9Å c: 97Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.176 not available

Quick links

Citations

56 review citations

The leucine-rich repeat: a versatile binding motif.
Kobe et al. (1994)
55 more

25 mentions without citation

Architecture and function of metallopeptidase catalytic domains.
Cerdà-Costa et al. (2014)
24 more