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2HML

Crystal Structure of the Naphthalene 1,2-Dioxygenase F352V Mutant Bound to Phenanthrene.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0018625molecular_functionnaphthalene 1,2-dioxygenase activity
A0019439biological_processobsolete aromatic compound catabolic process
A0044237biological_processcellular metabolic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0006725biological_processobsolete cellular aromatic compound metabolic process
B0019380biological_process3-phenylpropionate catabolic process
B0019439biological_processobsolete aromatic compound catabolic process
B0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 450
ChainResidue
AHIS208
AHIS213
AASP362
APEY701
AHOH753

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 704
ChainResidue
AHOH966
ALEU128
AASN129
ALYS130
ALYS131

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 709
ChainResidue
BGLN63
BGLN65
BHOH765
BHOH804
BHOH848

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 710
ChainResidue
BGLY59
BSER60
BGLU167
BLYS172

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 713
ChainResidue
ALYS245
ATRP439
AHIS440
AHOH884
AHOH928

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 714
ChainResidue
ATHR87
ASER90
ATHR368
AHOH794
AHOH835
AHOH963
BARG148
BHOH844

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES A 714
ChainResidue
ACYS81
AHIS83
AARG84
ACYS101
AHIS104
ATRP106

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEY A 701
ChainResidue
AASN201
AASP205
AHIS208
AVAL209
AASN297
AFE450
AHOH734
AHOH753

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO A 702
ChainResidue
ALEU31
APHE35
AALA36
AMET59
AGLY60
AILE61
AASP62
APHE152
ATYR376
AGLN377

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 703
ChainResidue
AHIS18
AVAL80
ACYS81
AARG82
ASER381
AASP382
AHOH732
AHOH798
AHOH808

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 705
ChainResidue
BTYR88
BGLN102
BMET191
BVAL192
BPHE193
BHOH732
BHOH733

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 706
ChainResidue
BASN91
BGLN94
BHOH762
BHOH828

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 707
ChainResidue
BARG138
BALA158
BGLU160
BPHE177
BVAL178
BASP179
BHOH727

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 708
ChainResidue
APRO49
AALA50
AASP53
AHOH847
BARG78
BTYR79
BLYS80
BLEU81

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 711
ChainResidue
APRO118
APHE119
AHOH892
AHOH1068

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 712
ChainResidue
BHOH849
BGLU83
BALA84
BASN86
BHOH797

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 715
ChainResidue
AGLU24
ALYS374
AHOH756
AHOH931
AHOH958

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 716
ChainResidue
ATHR56
AGLU92
APRO186
ALYS188
BGLU70
BARG183

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 717
ChainResidue
AARG342
AASP346
AHOH747
AHOH890
BASN82
BHOH849

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 718
ChainResidue
AVAL190
BGLN186
BTHR187
BHIS188

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 719
ChainResidue
BLEU10
BVAL11
BSER12
BLYS113

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 720
ChainResidue
ALYS136
ATYR376
AGLN377
AHOH758
AHOH1109

site_idCC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 721
ChainResidue
ASER73
AILE74
AVAL141
AHOH967

site_idCC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 722
ChainResidue
AVAL9
ASER10
AGLU11
AGLU442
AHOH846
AHOH1041

site_idCC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 723
ChainResidue
AHIS29
ALYS32

Functional Information from PROSITE/UniProt
site_idPS00570
Number of Residues24
DetailsRING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGktlvsveaGNakgfvCsYH
ChainResidueDetails
ACYS81-HIS104

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PDB entries from 2024-06-12

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