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7C8Z

Crystal structure of salicylate 5-hydroxylase NagGH (a Rieske non-heme iron-dependent monooxgenase)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0019439biological_processobsolete aromatic compound catabolic process
A0034785molecular_functionsalicylate 5-hydroxylase activity
A0044237biological_processcellular metabolic process
A0046244biological_processsalicylic acid catabolic process
A0046872molecular_functionmetal ion binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
A1902494cellular_componentcatalytic complex
B0004497molecular_functionmonooxygenase activity
B0006725biological_processobsolete cellular aromatic compound metabolic process
B0019439biological_processobsolete aromatic compound catabolic process
B0034785molecular_functionsalicylate 5-hydroxylase activity
B0046244biological_processsalicylic acid catabolic process
B1902494cellular_componentcatalytic complex
C0004497molecular_functionmonooxygenase activity
C0005506molecular_functioniron ion binding
C0019439biological_processobsolete aromatic compound catabolic process
C0034785molecular_functionsalicylate 5-hydroxylase activity
C0044237biological_processcellular metabolic process
C0046244biological_processsalicylic acid catabolic process
C0046872molecular_functionmetal ion binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
C1902494cellular_componentcatalytic complex
D0004497molecular_functionmonooxygenase activity
D0006725biological_processobsolete cellular aromatic compound metabolic process
D0019439biological_processobsolete aromatic compound catabolic process
D0034785molecular_functionsalicylate 5-hydroxylase activity
D0046244biological_processsalicylic acid catabolic process
D1902494cellular_componentcatalytic complex
E0004497molecular_functionmonooxygenase activity
E0005506molecular_functioniron ion binding
E0019439biological_processobsolete aromatic compound catabolic process
E0034785molecular_functionsalicylate 5-hydroxylase activity
E0044237biological_processcellular metabolic process
E0046244biological_processsalicylic acid catabolic process
E0046872molecular_functionmetal ion binding
E0051537molecular_function2 iron, 2 sulfur cluster binding
E1902494cellular_componentcatalytic complex
F0004497molecular_functionmonooxygenase activity
F0006725biological_processobsolete cellular aromatic compound metabolic process
F0019439biological_processobsolete aromatic compound catabolic process
F0034785molecular_functionsalicylate 5-hydroxylase activity
F0046244biological_processsalicylic acid catabolic process
F1902494cellular_componentcatalytic complex
G0004497molecular_functionmonooxygenase activity
G0005506molecular_functioniron ion binding
G0019439biological_processobsolete aromatic compound catabolic process
G0034785molecular_functionsalicylate 5-hydroxylase activity
G0044237biological_processcellular metabolic process
G0046244biological_processsalicylic acid catabolic process
G0046872molecular_functionmetal ion binding
G0051537molecular_function2 iron, 2 sulfur cluster binding
G1902494cellular_componentcatalytic complex
H0004497molecular_functionmonooxygenase activity
H0006725biological_processobsolete cellular aromatic compound metabolic process
H0019439biological_processobsolete aromatic compound catabolic process
H0034785molecular_functionsalicylate 5-hydroxylase activity
H0046244biological_processsalicylic acid catabolic process
H1902494cellular_componentcatalytic complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue FES A 501
ChainResidue
ACYS91
AHIS93
AARG94
ACYS111
AHIS114

site_idAC2
Number of Residues5
Detailsbinding site for residue FE A 502
ChainResidue
AHOH614
AASN218
AHIS224
AHIS229
AASP370

site_idAC3
Number of Residues5
Detailsbinding site for residue FES C 501
ChainResidue
CCYS91
CHIS93
CARG94
CCYS111
CHIS114

site_idAC4
Number of Residues3
Detailsbinding site for residue FE C 502
ChainResidue
CHIS224
CHIS229
CASP370

site_idAC5
Number of Residues6
Detailsbinding site for residue FES E 501
ChainResidue
ECYS91
EHIS93
EARG94
ECYS111
EHIS114
ETRP116

site_idAC6
Number of Residues3
Detailsbinding site for residue FE E 502
ChainResidue
EHIS224
EHIS229
EASP370

site_idAC7
Number of Residues6
Detailsbinding site for residue FES G 501
ChainResidue
GCYS91
GHIS93
GARG94
GCYS111
GHIS114
GTRP116

site_idAC8
Number of Residues4
Detailsbinding site for residue FE G 502
ChainResidue
GHIS224
GHIS229
GASP370
GHOH609

Functional Information from PROSITE/UniProt
site_idPS00570
Number of Residues24
DetailsRING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CaHRGmrfcrerhGNakdffCpYH
ChainResidueDetails
ACYS91-HIS114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O85673, ECO:0000255|PROSITE-ProRule:PRU00628
ChainResidueDetails
ECYS91
EHIS93
ECYS111
EHIS114
GCYS91
GHIS93
GCYS111
GHIS114
CCYS91
CHIS93
CCYS111
CHIS114
ACYS91
AHIS93
ACYS111
AHIS114

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O85673
ChainResidueDetails
EASP370
GHIS224
GHIS229
GASP370
CHIS229
CASP370
EHIS224
EHIS229
AHIS224
AHIS229
AASP370
CHIS224

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PDB entries from 2024-06-12

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