Structure of PDB 3b8i Chain B

Receptor sequence
>3b8iB (length=283) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
RASHHELRAMFRALLDSSRCYHTASVFDPMSARIAADLGFECGILGGSVA
SLQVLAAPDFALITLSEFVEQATRIGRVARLPVIADADHGYGNALNVMRT
VVELERAGIAALTIEDTLLPAQFGRKSTDLICVEEGVGKIRAALEARVDP
ALTIIARTNAELIDVDAVIQRTLAYQEAGADGICLVGVRDFAHLEAIAEH
LHIPLMLVTYGNPQLRDDARLARLGVRVVVNGHAAYFAAIKATYDCLREE
RGAVASDLTASELSKKYTFPEEYQAWARDYMEV
3D structure
PDB3b8i Structure and function of PA4872 from Pseudomonas aeruginosa, a novel class of oxaloacetate decarboxylase from the PEP mutase/isocitrate lyase superfamily.
ChainB
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) I44 G46 G47 S48 D59 D86 D88 T113 E115 A121 F123 G124 R157 V186 M206
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 B S50 D88 H235 S48 D86 H233 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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