Structure of PDB 2buz Chain A

Receptor sequence
>2buzA (length=202) Species: 62977 (Acinetobacter baylyi ADP1) [Search protein sequence]
ELKETPSQTGGPYVHIGLLPKQANIEVFEHNLDNNLVQDNTQGQRIRLEG
QVFDGLGLPLRDVLIEIWQADTNGVYPSQADTQGKQVDPNFLGWGRTGAD
FGTGFWSFNTIKPGAVPGRKGSTQAPHISLIIFAHGINIGLHTRVYFDDE
AEANAKDPVLNSIEWATRRQTLVAKREERDGEVVYRFDIRIQGENETVFF
DI
3D structure
PDB2buz Crystallographic Studies of Intradiol Dioxygenases
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y79 V114 Q122 H125 S127
Catalytic site (residue number reindexed from 1) Y76 V116 Q124 H127 S129
Enzyme Commision number 1.13.11.3: protocatechuate 3,4-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 4NC A P15 Y16 P12 Y13
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008199 ferric iron binding
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0018578 protocatechuate 3,4-dioxygenase activity
GO:0051213 dioxygenase activity
Biological Process
GO:0009056 catabolic process
GO:0042952 beta-ketoadipate pathway

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Molecular Function
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Biological Process
External links
PDB RCSB:2buz, PDBe:2buz, PDBj:2buz
PDBsum2buz
PubMed
UniProtP20371|PCXA_ACIAD Protocatechuate 3,4-dioxygenase alpha chain (Gene Name=pcaG)

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