Structure of PDB 2xsh Chain G

Receptor sequence
>2xshG (length=433) Species: 266265 (Paraburkholderia xenovorans LB400) [Search protein sequence]
NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRSWLLLGHESHV
PETGDFLATYMGEDPVVMVRQKDKSIKVFLNQCRHRGMRICRSDAGNAKA
FTCSYHGWAYDIAGKLVNVPFEKEAFFDKAEWGPLQARVATYKGLVFANW
DVQAPDLETYLGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ
FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFRAAWGGHGSGW
YVDEPGSLLAVMGPKVTQYWTEGPAAELAEQRLGHTGMPVRRMVGQHMTI
FPTCSFLPAMNNIRIWHPRGPNEIEVWAFTLVDADAPAEIKEEYRRHNIR
NFSAGGVFEQDDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP
GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP
3D structure
PDB2xsh Structural Insight Into the Expanded Pcb-Degrading Abilities of a Biphenyl Dioxygenase Obtained by Directed Evolution.
ChainG
Resolution2.29 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H123 D230 H233 H239 D388
Catalytic site (residue number reindexed from 1) H106 D204 H207 H213 D362
Enzyme Commision number 1.14.12.18: biphenyl 2,3-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 FES G C100 H102 R103 C120 Y122 H123 W125 C83 H85 R86 C103 Y105 H106 W108
BS02 FE2 G Q226 H233 H239 D388 Q200 H207 H213 D362
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0018687 biphenyl 2,3-dioxygenase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:0009056 catabolic process
GO:0044237 cellular metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2xsh, PDBe:2xsh, PDBj:2xsh
PDBsum2xsh
PubMed21073881
UniProtP37333|BPHA_PARXL Biphenyl dioxygenase subunit alpha (Gene Name=bphA)

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