Structure of PDB 1q0c Chain B

Receptor sequence
>1q0cB (length=319) Species: 47914 (Brevibacterium fuscum) [Search protein sequence]
EIPKPVAPAPDILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYL
RSFEEFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAYYQELGCRTER
RKDGFVKGIGDALRVEDPLGFPYEFFFETTHVERLHMRYDLYSAGELVRL
DHFNQVTPDVPRGRKYLEDLGFRVTEDIQDDEGTTYAAWMHRKGTVHDTA
LTGGNGPRLHHVAFSTHEKHNIIQICDKMGALRISDRIERGPGRHGVSNA
FYLYILDPDNHRIEIYTQDYYTGDPDNPTITWNVHDNQRRDWWGNPVVPS
WYTEASKVLDLDGNVQEII
3D structure
PDB1q0c Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases.
ChainB
Resolution2.1 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 FE B H155 H214 E267 H152 H211 E264
BS02 DHY B H155 W192 H200 H214 R243 H248 V250 S251 Y257 E267 R293 W304 H152 W189 H197 H211 R240 H245 V247 S248 Y254 E264 R290 W301
Gene Ontology
Molecular Function
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity

View graph for
Molecular Function
External links
PDB RCSB:1q0c, PDBe:1q0c, PDBj:1q0c
PDBsum1q0c
PubMed15028678
UniProtQ45135

[Back to BioLiP]