Structure of PDB 1o5q Chain D

Receptor sequence
>1o5qD (length=268) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium) [Search protein sequence]
HSPGQAFRAALAKENPLQIVGAINANHALLAQRAGYQAIYLSGGGVAAGS
LGLPDLGISTLDDVLTDIRRITDVCPLPLLVDADIGFGSSAFNVARTVKS
IAKAGAAALHIEDQVAIVSKEEMVDRIRAAVDARTDPNFVIMARTDALAV
EGLEAALDRAQAYVDAGADMLFPEAITELSMYRRFADVAQVPILANITEF
GATPLFTTDELRSAHVAMALYPLSAFRAMNRAAEKVYTVLRQEGTQKNVI
DIMQTRNELYESINYYQF
3D structure
PDB1o5q Crystal structure of Salmonella typhimurium 2-methylisocitrate lyase (PrpB) and its complex with pyruvate and Mg(2+)
ChainD
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y43 S45 G46 G47 D58 D85 D87 H113 E115 R158 E188 N210 T217 L219
Catalytic site (residue number reindexed from 1) Y40 S42 G43 G44 D55 D82 D84 H110 E112 R144 E174 N196 T203 L205
Enzyme Commision number 4.1.3.30: methylisocitrate lyase.
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 PYR D Y43 S45 G47 D85 R158 Y40 S42 G44 D82 R144
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0016833 oxo-acid-lyase activity
GO:0046421 methylisocitrate lyase activity
GO:0046872 metal ion binding
GO:0140677 molecular function activator activity
Biological Process
GO:0019629 propionate catabolic process, 2-methylcitrate cycle

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Molecular Function
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Biological Process
External links
PDB RCSB:1o5q, PDBe:1o5q, PDBj:1o5q
PDBsum1o5q
PubMed14575713
UniProtQ56062|PRPB_SALTY 2-methylisocitrate lyase (Gene Name=prpB)

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