Structure of PDB 3dhg Chain D

Receptor sequence

>3dhgD (length=492) Species: 300 (Pseudomonas mendocina)

AMHPRKDWYELTRATNWTPSYVTEEQLFPERMSGHMGIPLEKWESYDEPY
KTSYPEYVSIQREKDAGAYSVKAALERAKIYENSDPGWISTLKSHYGAIA
VGEYAAVTGEGRMARFSKAPGNRNMATFGMMDELRHGQLQLFFPHEYCKK
DRQFDWAWRAYHSNEWAAIAAKHFFDDIITGRDAISVAIMLTFSFETGFT
NMQFLGLAADAAEAGDYTFANLISSIQTDESRHAQQGGPALQLLIENGKR
EEAQKKVDMAIWRAWRLFAVLTGPVMDYYTPLEDRSQSFKEFMYEWIIGQ
FERSLIDLGLDKPWYWDLFLKDIDELHHSYHMGVWYWRTTAWWNPAAGVT
PEERDWLEEKYPGWNKRWGRCWDVITENVLNDRMDLVSPETLPSVCNMSQ
IPLVGVPGDDWNIEVFSLEHNGRLYHFGSEVDRWVFQQDPVQYQNHMNIV
DRFLAGQIQPMTLEGALKYMGFQSIEEMGKDAHDFAWADKCK

3D structure

• PDB: 3dhg Structural consequences of effector protein complex formation in a diiron hydroxylase.
• Chain: D
• Resolution: 1.85 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E104 E134 H137 E197 E231 H234
• Catalytic site (residue number reindexed from 1): E103 E133 H136 E196 E230 H233
• Enzyme Commision number: 1.14.13.236: toluene 4-monooxygenase.

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	FE	D	E134 E197 E231 H234	E133 E196 E230 H233
BS02	FE	D	E104 E134 H137	E103 E133 H136

Gene Ontology

Molecular Function

• GO:0004497 monooxygenase activity
• GO:0016491 oxidoreductase activity
• GO:0018638 toluene 4-monooxygenase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0009056 catabolic process
• GO:0042203 toluene catabolic process

External links

• PDB: RCSB:3dhg, PDBe:3dhg, PDBj:3dhg
• PDBsum: 3dhg
• PubMed: 19033467
• UniProt: Q00456|TMOA_PSEME Toluene-4-monooxygenase system, hydroxylase component subunit alpha (Gene Name=tmoA)