Structure of PDB 1lgt Chain A

Receptor sequence
>1lgtA (length=287) Species: 266265 (Paraburkholderia xenovorans LB400) [Search protein sequence]
SIRSLGYMGFAVSDVAAWRSFLTQKLGLMEAGTTDNGDLFRIDSRAWRIA
VQQGEVDDLAFAGYEVADAAGLAQMADKLKQAGIAVTTGDASLARRRGVT
GLITFADPFGLPLEIYYGASEVFEKPFLPGAAVSGFLTGEQGLGHFVRCV
PDSDKALAFYTDVLGFQLSDVIDMKMGPDVTVPAYFLHCNERHHTLAIAA
FPLPKRIHHFMLEVASLDDVGFAFDRVDADGLITSTLGRHTNDHMVSFYA
STPSGVEVEYGWSARTVDRSWVVVRHDSPSMWGHKSV
3D structure
PDB1lgt Identification and analysis of a bottleneck in PCB biodegradation
ChainA
Resolution1.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.13.11.39: biphenyl-2,3-diol 1,2-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 FE2 A H146 H210 E260 H145 H209 E259
BS02 FE2 A Q168 H189 Q167 H188
BS03 BP3 A H146 V148 M175 F187 H195 F202 H210 H241 N243 Y250 E260 H145 V147 M174 F186 H194 F201 H209 H240 N242 Y249 E259 MOAD: Kd=0.8uM
PDBbind-CN: -logKd/Ki=6.10,Kd=0.8uM
BS04 BP3 A L204 P205 K206 G256 E258 L203 P204 K205 G255 E257 MOAD: Kd=0.8uM
PDBbind-CN: -logKd/Ki=6.10,Kd=0.8uM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005506 iron ion binding
GO:0008198 ferrous iron binding
GO:0018583 biphenyl-2,3-diol 1,2-dioxygenase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0009056 catabolic process
GO:0042178 xenobiotic catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1lgt, PDBe:1lgt, PDBj:1lgt
PDBsum1lgt
PubMed12415290
UniProtP47228|BPHC_PARXL Biphenyl-2,3-diol 1,2-dioxygenase (Gene Name=bphC)

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