› 2bdi

X-ray diffraction
3Å resolution

Human Kallikrein 4 complex with cobalt and p-aminobenzamidine

Released:
DOI: 10.2210/pdb2bdi/pdb
PDB entry 2bdi coloured by chain, front view.
PDB entry 2bdi coloured by chain, side view.
PDB entry 2bdi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of human tissue kallikrein 4: activity modulation by a specific zinc binding site.
Debela M, Magdolen V, Grimminger V, Sommerhoff C, Messerschmidt A, Huber R, Friedrich R, Bode W, Goettig P
J Mol Biol 362 1094-107 (2006)
PMID: 16950394

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195272 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kallikrein-4 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 223 amino acids
Theoretical weight: 23.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y5K2 (Residues: 31-253; Coverage: 98%)
Gene names: EMSP1, KLK4, PRSS17, PSTS
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand CO 4 x CO
Ligand PBZ 16 x PBZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P21
Unit cell:
a: 147.05Å b: 73.86Å c: 154.38Å
α: 90° β: 102.41° γ: 90°
R-values:
R R work R free
0.258 0.258 0.296
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Unleashing the therapeutic potential of human kallikrein-related serine proteases.
Prassas et al. (2015)
12 more

2 mentions without citation

The expanding diversity of serine hydrolases.
Botos et al. (2007)
1 more