PDB 4ghd

PDB Information

PDB4GHD
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
Resolution1.850
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
4ghdA01 10 Nov, 2012 3.10.180.10 Assigned
4ghdA02 10 Nov, 2012 3.10.180.10 Assigned
4ghdA03 10 Nov, 2012 4.10.1270.10 Assigned
4ghdB01 10 Nov, 2012 3.10.180.10 Assigned
4ghdB02 10 Nov, 2012 3.10.180.10 Assigned
4ghdB03 10 Nov, 2012 4.10.1270.10 Assigned
4ghdC01 10 Nov, 2012 3.10.180.10 Assigned
4ghdC02 10 Nov, 2012 3.10.180.10 Assigned
4ghdC03 10 Nov, 2012 4.10.1270.10 Assigned
4ghdD01 10 Nov, 2012 3.10.180.10 Assigned
4ghdD02 10 Nov, 2012 3.10.180.10 Assigned
4ghdD03 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