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5BRT

Crystal Structure of 2-hydroxybiphenyl 3-monooxygenase from Pseudomonas azelaica with 2-hydroxybiphenyl in the active site

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004497molecular_functionmonooxygenase activity
A0016491molecular_functionoxidoreductase activity
A0016709molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
A0071949molecular_functionFAD binding
B0000166molecular_functionnucleotide binding
B0004497molecular_functionmonooxygenase activity
B0016491molecular_functionoxidoreductase activity
B0016709molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
B0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues30
Detailsbinding site for residue FAD A 601
ChainResidue
AGLY13
ASER47
AGLN120
ATHR142
AGLU143
ATYR144
AALA177
AASP178
AGLY179
AARG242
ATRP293
AALA14
AGLY312
AASP313
APRO320
ASER329
AHOH736
AHOH753
AHOH781
AHOH794
AHOH861
AHOH876
AGLY15
AHOH884
APRO16
AALA17
AASN36
AARG37
ATRP38
AARG46

site_idAC2
Number of Residues7
Detailsbinding site for residue CH9 A 602
ChainResidue
AHIS48
ATRP97
AMET223
APRO320
AMET321
AGLY322
AGLY427

site_idAC3
Number of Residues30
Detailsbinding site for residue FAD B 601
ChainResidue
BGLY13
BALA14
BGLY15
BPRO16
BALA17
BASN36
BARG37
BTRP38
BARG46
BSER47
BGLN120
BTHR142
BTYR144
BALA177
BASP178
BGLY179
BARG242
BTRP293
BGLY312
BASP313
BPRO320
BSER329
BHOH707
BHOH714
BHOH719
BHOH778
BHOH812
BHOH832
BHOH871
BHOH925

site_idAC4
Number of Residues9
Detailsbinding site for residue CH9 B 602
ChainResidue
BHIS48
BTRP97
BMET223
BVAL253
BPRO320
BMET321
BGLY322
BGLY427
BLEU428

219869

PDB entries from 2024-05-15

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