PDB Information

PDB4GHE
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
Resolution1.600
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
4gheA01 10 Nov, 2012 3.10.180.10 Assigned
4gheA02 10 Nov, 2012 3.10.180.10 Assigned
4gheA03 10 Nov, 2012 4.10.1270.10 Assigned
4gheB01 10 Nov, 2012 3.10.180.10 Assigned
4gheB02 10 Nov, 2012 3.10.180.10 Assigned
4gheB03 10 Nov, 2012 4.10.1270.10 Assigned
4gheC01 10 Nov, 2012 3.10.180.10 Assigned
4gheC02 10 Nov, 2012 3.10.180.10 Assigned
4gheC03 10 Nov, 2012 4.10.1270.10 Assigned
4gheD01 10 Nov, 2012 3.10.180.10 Assigned
4gheD02 10 Nov, 2012 3.10.180.10 Assigned
4gheD03 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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