Structure of PDB 4ghh Chain D

Receptor sequence
>4ghhD (length=359) Species: 47914 (Brevibacterium fuscum) [Search protein sequence]
EIPKPVAPAPDILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYL
RSFEEFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAYYQELGCRTER
RKDGFVKGIGDALRVEDPLGFPYEFFFETTHVERLHMRYDLYSAGELVRL
DHFNQVTPDVPRGRKYLEDLGFRVTEDIQDDEGTTYAAWMHRKGTVHDTA
LTGGNGPRLHHVAFSTHEKHNIIQICDKMGALRISDRIERGPGRHGVSNA
FYLYILDPDNHRIEIYTQDYYTGDPDNPTITWNVHDNQRRDWWGNPVVPS
WYTEASKVLDLDGNVQEIIERTDDSELEVTIGADGFSFTRAGDEDGSYHG
QASKGFKLG
3D structure
PDB4ghh Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation.
ChainD
Resolution1.55 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) H152 H197 H211 H245 Y254 E264
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 D H155 H214 E267 H152 H211 E264
BS02 4NC D H155 W192 H200 H214 H248 V250 Y257 E267 R293 H152 W189 H197 H211 H245 V247 Y254 E264 R290
Gene Ontology
Molecular Function
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity

View graph for
Molecular Function
External links
PDB RCSB:4ghh, PDBe:4ghh, PDBj:4ghh
PDBsum4ghh
PubMed23066739
UniProtQ45135

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