PDB 4ghh

PDB Information

PDB4GHH
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
Resolution1.550
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
4ghhA01 10 Nov, 2012 3.10.180.10 Assigned
4ghhA02 10 Nov, 2012 3.10.180.10 Assigned
4ghhA03 10 Nov, 2012 4.10.1270.10 Assigned
4ghhB01 10 Nov, 2012 3.10.180.10 Assigned
4ghhB02 10 Nov, 2012 3.10.180.10 Assigned
4ghhB03 10 Nov, 2012 4.10.1270.10 Assigned
4ghhC01 10 Nov, 2012 3.10.180.10 Assigned
4ghhC02 10 Nov, 2012 3.10.180.10 Assigned
4ghhC03 10 Nov, 2012 4.10.1270.10 Assigned
4ghhD01 10 Nov, 2012 3.10.180.10 Assigned
4ghhD02 10 Nov, 2012 3.10.180.10 Assigned
4ghhD03 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
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