Structure of PDB 2iga Chain C

Receptor sequence
>2igaC (length=359) Species: 47914 (Brevibacterium fuscum) [Search protein sequence]
EIPKPVAPAPDILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYL
RSFEEFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAYYQELGCRTER
RKDGFVKGIGDALRVEDPLGFPYEFFFETTHVERLHMRYDLYSAGELVRL
DHFNQVTPDVPRGRKYLEDLGFRVTEDIQDDEGTTYAAWMHRKGTVHDTA
LTGGNGPRLHHVAFSTHEKHNIIQICDKMGALRISDRIERGPGRHGVSNA
FYLYILDPDNHRIEIYTQDYYTGDPDNPTITWNVHDNQRRDWWGNPVVPS
WYTEASKVLDLDGNVQEIIERTDDSELEVTIGADGFSFTRAGDEDGSYHG
QASKGFKLG
3D structure
PDB2iga Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates
ChainC
Resolution1.95 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) 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 C H155 H214 E267 H152 H211 E264
BS02 XX2 C H155 W192 H200 H214 H248 V250 S251 Y257 E267 R293 H152 W189 H197 H211 H245 V247 S248 Y254 E264 R290
BS03 OXY C H155 N157 H200 H152 N154 H197
Gene Ontology
Molecular Function
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity

View graph for
Molecular Function
External links
PDB RCSB:2iga, PDBe:2iga, PDBj:2iga
PDBsum2iga
PubMed17446402
UniProtQ45135

[Back to BioLiP]