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6VSH

Crystal structure of apo Dicamba Monooxygenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0009056biological_processcatabolic process
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0046872molecular_functionmetal ion binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0004497molecular_functionmonooxygenase activity
B0009056biological_processcatabolic process
B0016491molecular_functionoxidoreductase activity
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0046872molecular_functionmetal ion binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
C0004497molecular_functionmonooxygenase activity
C0009056biological_processcatabolic process
C0016491molecular_functionoxidoreductase activity
C0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C0046872molecular_functionmetal ion binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue FES A 501
ChainResidue
ACYS49
AHIS51
AARG52
ACYS68
AHIS71
ALEU73

site_idAC2
Number of Residues6
Detailsbinding site for residue FES B 501
ChainResidue
BCYS68
BHIS71
BLEU73
BCYS49
BHIS51
BARG52

site_idAC3
Number of Residues5
Detailsbinding site for residue FES C 501
ChainResidue
CCYS49
CHIS51
CCYS68
CHIS71
CLEU73

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsBINDING: BINDING => ECO:0000269|PubMed:19616009, ECO:0000269|PubMed:19616011, ECO:0007744|PDB:3GB4, ECO:0007744|PDB:3GKE, ECO:0007744|PDB:3GL0, ECO:0007744|PDB:3GL2, ECO:0007744|PDB:3GOB, ECO:0007744|PDB:3GTE, ECO:0007744|PDB:3GTS
ChainResidueDetails
ACYS49
BCYS68
BHIS71
BHIS160
BHIS165
BASP294
CCYS49
CHIS51
CCYS68
CHIS71
CHIS160
AHIS51
CHIS165
CASP294
ACYS68
AHIS71
AHIS160
AHIS165
AASP294
BCYS49
BHIS51

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19616009, ECO:0000269|PubMed:19616011, ECO:0007744|PDB:3GB4, ECO:0007744|PDB:3GKE, ECO:0007744|PDB:3GL0, ECO:0007744|PDB:3GL2, ECO:0007744|PDB:3GOB, ECO:0007744|PDB:3GTS
ChainResidueDetails
AASN230
AHIS251
BASN230
BHIS251
CASN230
CHIS251

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:19616009, ECO:0000269|PubMed:19616011, ECO:0007744|PDB:3GB4, ECO:0007744|PDB:3GKE, ECO:0007744|PDB:3GL0, ECO:0007744|PDB:3GL2, ECO:0007744|PDB:3GTS
ChainResidueDetails
ATRP285
BTRP285
CTRP285

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Plays a role in the stabilization of the metal coordination => ECO:0000269|PubMed:19616009
ChainResidueDetails
AASN154
BASN154
CASN154

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PDB entries from 2024-11-06

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