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2V27

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
A0009072biological_processaromatic amino acid metabolic process
A0016491molecular_functionoxidoreductase activity
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
A0019293biological_processtyrosine biosynthetic process, by oxidation of phenylalanine
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0004505molecular_functionphenylalanine 4-monooxygenase activity
B0005506molecular_functioniron ion binding
B0006559biological_processL-phenylalanine catabolic process
B0009072biological_processaromatic amino acid metabolic process
B0016491molecular_functionoxidoreductase activity
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
B0019293biological_processtyrosine biosynthetic process, by oxidation of phenylalanine
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A1268
ChainResidue
AHIS122
AHIS127
AGLU167
AHOH2231
AHOH2273

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1269
ChainResidue
AHOH2409
AARG212
AHIS257
AGLU258
AHOH2408

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B3008
ChainResidue
BHIS122
BHIS127
BGLU167
BHOH2201
BHOH2357

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B3009
ChainResidue
BTYR80
BARG93
BLYS99
BHOH2358
BHOH2359

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

239492

PDB entries from 2025-07-30

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