Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2V28

Apo structure of the cold active phenylalanine hydroxylase from Colwellia psychrerythraea 34H

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0004505molecular_functionphenylalanine 4-monooxygenase activity
A0005506molecular_functioniron ion binding
A0006559biological_processL-phenylalanine catabolic process
A0006571biological_processL-tyrosine biosynthetic process
A0009072biological_processaromatic amino acid metabolic process
A0016714molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
B0004497molecular_functionmonooxygenase activity
B0004505molecular_functionphenylalanine 4-monooxygenase activity
B0005506molecular_functioniron ion binding
B0006559biological_processL-phenylalanine catabolic process
B0006571biological_processL-tyrosine biosynthetic process
B0009072biological_processaromatic amino acid metabolic process
B0016714molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A1268
ChainResidue
AARG212
AHIS257
AGLU258
AHOH2291
AHOH2364
AHOH2365

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B1268
ChainResidue
BHOH2263
BHOH2264
BTYR80
BARG93
BLYS99

Functional Information from PROSITE/UniProt
site_idPS00367
Number of Residues12
DetailsBH4_AAA_HYDROXYL_1 Biopterin-dependent aromatic amino acid hydroxylases signature. PDifHEIFGHCP
ChainResidueDetails
APRO118-PRO129

253389

PDB entries from 2026-05-13

PDB statisticsPDBj update infoContact PDBjnumon