PDB 4ghf

PDB Information

PDB4GHF
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
Resolution1.670
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
4ghfA01 10 Nov, 2012 3.10.180.10 Assigned
4ghfA02 10 Nov, 2012 3.10.180.10 Assigned
4ghfA03 10 Nov, 2012 4.10.1270.10 Assigned
4ghfB01 10 Nov, 2012 3.10.180.10 Assigned
4ghfB02 10 Nov, 2012 3.10.180.10 Assigned
4ghfB03 10 Nov, 2012 4.10.1270.10 Assigned
4ghfC01 10 Nov, 2012 3.10.180.10 Assigned
4ghfC02 10 Nov, 2012 3.10.180.10 Assigned
4ghfC03 10 Nov, 2012 4.10.1270.10 Assigned
4ghfD01 10 Nov, 2012 3.10.180.10 Assigned
4ghfD02 10 Nov, 2012 3.10.180.10 Assigned
4ghfD03 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