Structure of PDB 2xso Chain M

Receptor sequence

>2xsoM (length=433) Species: 266265 (Paraburkholderia xenovorans LB400)

NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRSWLLLGHESHV
PETGDFLATYMGEDPVVMVRQKDKSIKVFLNQCRHRGMRICRSDAGNAKA
FTCSYHGWAYDIAGKLVNVPFEKEAFFDKAEWGPLQARVATYKGLVFANW
DVQAPDLETYLGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ
FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFRAAWGGHGSGW
YVDEPGSLLAVMGPKVTQYWTEGPAAELAEQRLGHTGMPVRRMVGQHMTI
FPTCSFLPAMNNIRIWHPRGPNEIEVWAFTLVDADAPAEIKEEYRRHNIR
NFSAGGVFEQDDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP
GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP

3D structure

• PDB: 2xso Structural Insight Into the Expanded Pcb-Degrading Abilities of a Biphenyl Dioxygenase Obtained by Directed Evolution.
• Chain: M
• Resolution: 2.2 Å

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	M	C100 H102 R103 C120 Y122 H123 W125	C83 H85 R86 C103 Y105 H106 W108
BS02	FE2	M	H233 H239 D388	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

External links

• PDB: RCSB:2xso, PDBe:2xso, PDBj:2xso
• PDBsum: 2xso
• PubMed: 21073881
• UniProt: P37333|BPHA_PARXL Biphenyl dioxygenase subunit alpha (Gene Name=bphA)