X-ray diffraction
2.7Å resolution

Crystal structure of DNA cross-link repair protein 1A in complex with ceftriaxone

Source organism: Homo sapiens
Entry authors: Newman JA, Aitkenhead H, Kupinska K, Burgess-Brown NA, Talon R, Krojer T, von Delft F, Arrowsmith CH, Edwards A, Bountra C, Gileadi O

Function and Biology Details

Reaction catalysed:
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
DNA cross-link repair 1A protein Chain: A
Molecule details ›
Chain: A
Length: 343 amino acids
Theoretical weight: 38.92 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
  • Canonical: Q6PJP8 (Residues: 698-1040; Coverage: 33%)
Gene names: DCLRE1A, KIAA0086, SNM1, SNM1A
Sequence domains: DNA repair metallo-beta-lactamase
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: P212121
Unit cell:
a: 51.356Å b: 58.495Å c: 112.538Å
α: 90° β: 90° γ: 90°
R R work R free
0.231 0.226 0.315
Expression system: Spodoptera frugiperda