PDB Information

PDB2X36
MethodX-RAY DIFFRACTION
Host OrganismESCHERICHIA COLI
Gene SourceHOMO SAPIENS
Primary Citation
Structure of the Catalytic Domain of the Human Mitochondrial Lon Protease: Proposed Relation of Oligomer Formation and Activity.
Garcia-Nafria, J., Ondrovicova, G., Blagova, E., Levdikov, V.M., Bauer, J.A., Suzuki, C.K., Kutejova, E., Wilkinson, A.J., Wilson, K.S.
Protein Sci.
HeaderHydrolase
Released2010-01-21
Resolution2.000
CATH Insert Date23 May, 2010

PDB Images (13)

PDB Prints

PDB Chains (6)

Chain ID Date inserted into CATH CATH Status
A 24 May, 2010 Chopped
B 24 May, 2010 Chopped
C 24 May, 2010 Chopped
D 24 May, 2010 Chopped
E 24 May, 2010 Chopped
F 24 May, 2010 Chopped

CATH Domains (6)

Domain ID Date inserted into CATH Superfamily CATH Status
2x36A01 08 Jun, 2010 3.30.230.10 Assigned
2x36B00 08 Jun, 2010 3.30.230.10 Assigned
2x36C01 08 Jun, 2010 3.30.230.10 Assigned
2x36D00 08 Jun, 2010 3.30.230.10 Assigned
2x36E00 08 Jun, 2010 3.30.230.10 Assigned
2x36F00 08 Jun, 2010 3.30.230.10 Assigned

UniProtKB Entries (6)

Accession Gene ID Taxon Description
P36776 LONM_HUMAN Homo sapiens Lon protease homolog, mitochondrial
P36776 LONM_HUMAN Homo sapiens Lon protease homolog, mitochondrial
P36776 LONM_HUMAN Homo sapiens Lon protease homolog, mitochondrial
P36776 LONM_HUMAN Homo sapiens Lon protease homolog, mitochondrial
P36776 LONM_HUMAN Homo sapiens Lon protease homolog, mitochondrial
P36776 LONM_HUMAN Homo sapiens Lon protease homolog, mitochondrial