Structure of PDB 2v27 Chain B

Receptor sequence

>2v27B (length=272) Species: 167879 (Colwellia psychrerythraea 34H)

GTKYVSKVPDEHGFIEWSTEENLIWQELFTRQIACIKDKACDEYHEGLAK
LNLPTDRIPQLDEVSKVLKVSTGWECYPVPALIGFGEFFRLLSEKKFPVA
TFIRSREEMDYLQEPDIFHEIFGHCPLLTNSSFANYTEAYGKMGLNATKE
QRVFLARLYWFTIEFGLLDTPKGLRIYGGGVLSSPGETDYAMNNTDVDRK
PFDILDVLRTPYRIDIMQPIYYMLTKVSDLDEIRKFEVDDIMELVAQAEA
LGLHEAKFPVKKASLEHHHHHH

3D structure

• PDB: 2v27 Structure of Phenylalanine Hydroxylase from Colwellia Psychrerythraea 34H, a Monomeric Cold Active Enzyme with Local Flexibility Around the Active Site and High Overall Stability.
• Chain: B
• Resolution: 1.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H122 H127 E167 S186
• Catalytic site (residue number reindexed from 1): H119 H124 E164 S183
• Enzyme Commision number: 1.14.16.1: phenylalanine 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	B	H122 H127 E167	H119 H124 E164

Gene Ontology

Molecular Function

• GO:0004497 monooxygenase activity
• GO:0004505 phenylalanine 4-monooxygenase activity
• GO:0005506 iron ion binding
• GO:0016714 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
• GO:0046872 metal ion binding

Biological Process

• GO:0006559 L-phenylalanine catabolic process
• GO:0009072 aromatic amino acid metabolic process
• GO:0019293 tyrosine biosynthetic process, by oxidation of phenylalanine

External links

• PDB: RCSB:2v27, PDBe:2v27, PDBj:2v27
• PDBsum: 2v27
• PubMed: 17537732
• UniProt: Q47XN7