› 7v5s

X-ray diffraction
3.02Å resolution

Crystal structure of human bleomycin hydrolase C73A mutant

Released:
DOI: 10.2210/pdb7v5s/pdb
PDB entry 7v5s coloured by chain, front view.
PDB entry 7v5s coloured by chain, side view.
PDB entry 7v5s coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The Structure-Function Relationship of Human Bleomycin Hydrolase: Mutation of a Cysteine Protease into a Serine Protease.
Zheng YZ, Cui J, Wang YL, Huang SJ, Lin EC, Huang SC, Rudolf JD, Yan X, Chang CY
Chembiochem 23 e202200186 (2022)
PMID: 35467071

Function and Biology Details

Reaction catalysed: 
Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred (1).
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171827 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bleomycin hydrolase Chain: A
Molecule details ›
Chain: A
Length: 475 amino acids
Theoretical weight: 54.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13867 (Residues: 1-455; Coverage: 100%)
Gene name: BLMH
Sequence domains: Peptidase C1-like family

Ligands and Environments

2 bound ligands:
Ligand PG4 1 x PG4
Ligand PGE 1 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: I4132
Unit cell:
a: 318.269Å b: 318.269Å c: 318.269Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.18 0.197
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Identification and classification of papain-like cysteine proteinases.
Ozhelvaci et al. (2023)