Structure of PDB 1kmy Chain A

Receptor sequence
>1kmyA (length=288) Species: 266265 (Paraburkholderia xenovorans LB400) [Search protein sequence]
SIRSLGYMGFAVSDVAAWRSFLTQKLGLMEAGTTDNGDLFRIDSRAWRIA
VQQGEVDDLAFAGYEVADAAGLAQMADKLKQAGIAVTTGDASLARRRGVT
GLITFADPFGLPLEIYYGASEVFEKPFLPGAAVSGFLTGEQGLGHFVRCV
PDSDKALAFYTDVLGFQLSDVIDMKMGPDVTVPAYFLHCNERHHTLAIAA
FPLPKRIHHFMLEVASLDDVGFAFDRVDADGLITSTLGRHTNDHMVSFYA
STPSGVEVEYGWSARTVDRSWVVVRHDSPSMWGHKSVR
3D structure
PDB1kmy Molecular basis for the stabilization and inhibition of 2, 3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol.
ChainA
Resolution2.0 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 BPY A H146 F187 H195 H210 H241 N243 Y250 E260 H145 F186 H194 H209 H240 N242 Y249 E259 MOAD: Kd=8uM
PDBbind-CN: -logKd/Ki=5.10,Kd=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:1kmy, PDBe:1kmy, PDBj:1kmy
PDBsum1kmy
PubMed9857017
UniProtP47228|BPHC_PARXL Biphenyl-2,3-diol 1,2-dioxygenase (Gene Name=bphC)

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