Structure of PDB 4ghg Chain B

Receptor sequence
>4ghgB (length=360) Species: 47914 (Brevibacterium fuscum) [Search protein sequence]
NEIPKPVAPAPDILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIY
LRSFEEFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAYYQELGCRTE
RRKDGFVKGIGDALRVEDPLGFPYEFFFETTHVERLHMRYDLYSAGELVR
LDHFNQVTPDVPRGRKYLEDLGFRVTEDIQDDEGTTYAAWMHRKGTVHDT
ALTGGNGPRLHHVAFSTHEKHNIIQICDKMGALRISDRIERGPGRHGVSN
AFYLYILDPDNHRIEIYTQDYYTGDPDNPTITWNVHDNQRRDWWGNPVVP
SWYTEASKVLDLDGNVQEIIERTDDSELEVTIGADGFSFTRAGDEDGSYH
GQASKGFKLG
3D structure
PDB4ghg Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation.
ChainB
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H155 H200 H214 H248 Y257 E267
Catalytic site (residue number reindexed from 1) H153 H198 H212 H246 Y255 E265
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 B H155 H214 E267 H153 H212 E265
BS02 CA B D184 E185 D182 E183
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

[Back to BioLiP]