PDB 4ghc

PDB Information

PDB4GHC
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
4ghcA01 10 Nov, 2012 3.10.180.10 Assigned
4ghcA02 10 Nov, 2012 3.10.180.10 Assigned
4ghcA03 10 Nov, 2012 4.10.1270.10 Assigned
4ghcB01 10 Nov, 2012 3.10.180.10 Assigned
4ghcB02 10 Nov, 2012 3.10.180.10 Assigned
4ghcB03 10 Nov, 2012 4.10.1270.10 Assigned
4ghcC01 10 Nov, 2012 3.10.180.10 Assigned
4ghcC02 10 Nov, 2012 3.10.180.10 Assigned
4ghcC03 10 Nov, 2012 4.10.1270.10 Assigned
4ghcD01 10 Nov, 2012 3.10.180.10 Assigned
4ghcD02 10 Nov, 2012 3.10.180.10 Assigned
4ghcD03 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