Structure of PDB 4ghg Chain C

Receptor sequence
>4ghgC (length=356) Species: 47914 (Brevibacterium fuscum) [Search protein sequence]
SNEIPKPVAPAPDILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQI
YLRSFEEFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAYYQELGCRT
ERRKDGFVKGIGDALRVEDPLGFPYEFFFETTHVERLHMRYDLYSAGELV
RLDHFNQVTPDVPRGRKYLEDLGFRVTEDIQDDEGTTYAAWMHRKGTVHD
TALTGGNGPRLHHVAFSTHEKHNIIQICDKMGALRISDRIERGPGRHGVS
NAFYLYILDPDNHRIEIYTQDYYTGDPDNPTITWNVHDNQRRDWWGNPVV
PSWYTEASKVLDLDGNVQEIIERTDDSELEVTIGADGFSFTRAGDEDGSY
HGQASK
3D structure
PDB4ghg Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation.
ChainC
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H155 H200 H214 H248 Y257 E267
Catalytic site (residue number reindexed from 1) H154 H199 H213 H247 Y256 E266
Enzyme Commision number 1.13.11.15: 3,4-dihydroxyphenylacetate 2,3-dioxygenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FE2 C H155 H214 E267 H154 H213 E266
BS02 DHY C H155 W192 H200 H214 R243 H248 V250 S251 Y257 E267 R293 H154 W191 H199 H213 R242 H247 V249 S250 Y256 E266 R292
Gene Ontology
Molecular Function
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity

View graph for
Molecular Function
External links
PDB RCSB:4ghg, PDBe:4ghg, PDBj:4ghg
PDBsum4ghg
PubMed23066739
UniProtQ45135

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