Structure of PDB 3b8i Chain E

Receptor sequence
>3b8iE (length=283) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
ASHHELRAMFRALLDSSRCYHTASVFDPMSARIAADLGFECGILGGSVAS
LQVLAAPDFALITLSEFVEQATRIGRVARLPVIADADHGYGNALNVMRTV
VELERAGIAALTIEDTLLPAQFGRKSTDLICVEEGVGKIRAALEARVDPA
LTIIARTNAELIDVDAVIQRTLAYQEAGADGICLVGVRDFAHLEAIAEHL
HIPLMLVTYGNPQLRDDARLARLGVRVVVNGHAAYFAAIKATYDCLREER
GAVASDLTASELSKKYTFPEEYQAWARDYMEVK
3D structure
PDB3b8i Structure and function of PA4872 from Pseudomonas aeruginosa, a novel class of oxaloacetate decarboxylase from the PEP mutase/isocitrate lyase superfamily.
ChainE
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I46 G48 G49 S50 D61 D88 D90 T115 E117 A123 F125 G126 R159 V188 M208
Catalytic site (residue number reindexed from 1) I43 G45 G46 S47 D58 D85 D87 T112 E114 A120 F122 G123 R156 V185 M205
Enzyme Commision number 4.1.1.112: oxaloacetate decarboxylase.
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 OXL E S50 D88 H235 S47 D85 H232 MOAD: Ki=4uM
BindingDB: Ki=43000nM
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0008948 oxaloacetate decarboxylase activity
GO:0016831 carboxy-lyase activity
GO:0016833 oxo-acid-lyase activity
GO:0046421 methylisocitrate lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006107 oxaloacetate metabolic process
GO:0019629 propionate catabolic process, 2-methylcitrate cycle
GO:0042866 pyruvate biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3b8i, PDBe:3b8i, PDBj:3b8i
PDBsum3b8i
PubMed18081320
UniProtQ9HUU1|OADC_PSEAE Oxaloacetate decarboxylase (Gene Name=PA4872)

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