Structure of PDB 4di8 Chain A

Receptor sequence
>4di8A (length=294) Species: 13689 (Sphingomonas paucimobilis) [Search protein sequence]
SLTNDERILSWNETPSKPRYTPPPGAIDAHCHVFGPMAQFPFSPKAKYLP
RDAGPDMLFALRDHLGFARNVIVQASCHGTDNAATLDAIARAQGKARGIA
VVDPAIDEAELAALHEGGMRGIRFNFLKRLVDDAPKDKFLEVAGRLPAGW
HVVIYFEADILEELRPFMDAIPVPIVIDHMGRPDVRQGPDGADMKAFRRL
LDSREDIWFKATCPDRLDPAGPPWDDFARSVAPLVADYADRVIWGTAWPH
PNMQDAIPDDGLVVDMIPRIAPTPELQHKMLVTNPMRLYWSEEM
3D structure
PDB4di8 Structure and Catalytic Mechanism of LigI: Insight into the Amidohydrolase Enzymes of cog3618 and Lignin Degradation.
ChainA
Resolution1.81 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A248
Catalytic site (residue number reindexed from 1) A247
Enzyme Commision number 3.1.1.57: 2-pyrone-4,6-dicarboxylate lactonase.
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 0GZ A H31 Y49 A76 S77 R124 R130 L131 Y156 R217 N253 H30 Y48 A75 S76 R123 R129 L130 Y155 R216 N252
BS02 0GY A H31 H33 Y49 A76 S77 R124 R130 L131 Y156 H180 R217 N253 H30 H32 Y48 A75 S76 R123 R129 L130 Y155 H179 R216 N252
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0047554 2-pyrone-4,6-dicarboxylate lactonase activity
Biological Process
GO:0009056 catabolic process
GO:0019619 3,4-dihydroxybenzoate catabolic process
GO:0046274 lignin catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4di8, PDBe:4di8, PDBj:4di8
PDBsum4di8
PubMed22475079
UniProtO87170|LIGI_SPHSK 2-pyrone-4,6-dicarboxylate hydrolase (Gene Name=ligI)

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