PDB 4ghg

PDB Information

PDB4GHG
MethodX-RAY DIFFRACTION
Host OrganismEscherichia coli
Gene SourceBrevibacterium fuscum
Primary Citation
Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation.
Kovaleva, E.G., Lipscomb, J.D.
Biochemistry
HeaderOxidoreductase
Released2012-08-07
Resolution1.500
CATH Insert Date04 Nov, 2012

PDB Images (17)

PDB Prints

PDB Chains (4)

Chain ID Date inserted into CATH CATH Status
A 05 Nov, 2012 Chopped
B 05 Nov, 2012 Chopped
C 05 Nov, 2012 Chopped
D 05 Nov, 2012 Chopped

CATH Domains (12)

Domain ID Date inserted into CATH Superfamily CATH Status
4ghgA01 10 Nov, 2012 3.10.180.10 Assigned
4ghgA02 10 Nov, 2012 3.10.180.10 Assigned
4ghgA03 10 Nov, 2012 4.10.1270.10 Assigned
4ghgB01 10 Nov, 2012 3.10.180.10 Assigned
4ghgB02 10 Nov, 2012 3.10.180.10 Assigned
4ghgB03 10 Nov, 2012 4.10.1270.10 Assigned
4ghgC01 10 Nov, 2012 3.10.180.10 Assigned
4ghgC02 10 Nov, 2012 3.10.180.10 Assigned
4ghgC03 10 Nov, 2012 4.10.1270.10 Assigned
4ghgD01 10 Nov, 2012 3.10.180.10 Assigned
4ghgD02 10 Nov, 2012 3.10.180.10 Assigned
4ghgD03 10 Nov, 2012 4.10.1270.10 Assigned

UniProtKB Entries (4)

Accession Gene ID Taxon Description
Q45135 Q45135_9MICO Brevibacterium fuscum Homoprotocatechuate 2,3-dioxygenase
Q45135 Q45135_9MICO Brevibacterium fuscum Homoprotocatechuate 2,3-dioxygenase
Q45135 Q45135_9MICO Brevibacterium fuscum Homoprotocatechuate 2,3-dioxygenase
Q45135 Q45135_9MICO Brevibacterium fuscum Homoprotocatechuate 2,3-dioxygenase