PDB Information

PDB4PVQ
MethodX-RAY DIFFRACTION
Host OrganismEscherichia coli
Gene SourceHomo sapiens
Primary Citation
Structures of apo and product-bound human L-asparaginase: insights into the mechanism of autoproteolysis and substrate hydrolysis.
Nomme, J., Su, Y., Konrad, M., Lavie, A.
Biochemistry
HeaderHydrolase
Released2014-03-18
Resolution2.130
CATH Insert Date30 Mar, 2014

PDB Images (5)

PDB Prints

PDB Chains (2)

Chain ID Date inserted into CATH CATH Status
A 31 Mar, 2014 Chopped
B 31 Mar, 2014 Chopped

CATH Domains (2)

Domain ID Date inserted into CATH Superfamily CATH Status
4pvqA00 25 Apr, 2014 Holding pen
4pvqB00 25 Apr, 2014 Holding pen

UniProtKB Entries (2)

Accession Gene ID Taxon Description
Q7L266 ASGL1_HUMAN Homo sapiens Isoaspartyl peptidase/L-asparaginase
Q7L266 ASGL1_HUMAN Homo sapiens Isoaspartyl peptidase/L-asparaginase