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6WND

Structure of the Rieske non-heme iron oxygenase GxtA with dideoxysaxitoxin bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0005506molecular_functioniron ion binding
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
C0005506molecular_functioniron ion binding
C0016491molecular_functionoxidoreductase activity
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
ACYS55
AHIS57
AARG58
ACYS74
AHIS77
ATRP79

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL A 502
ChainResidue
AGLU111
APRO47
AILE48
ACYS109

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 503
ChainResidue
AHIS139
ALYS140
ALYS263
AHOH609
CGOL504

site_idAC4
Number of Residues3
Detailsbinding site for residue GOL A 504
ChainResidue
ALYS144
AASP274
AGLU278

site_idAC5
Number of Residues2
Detailsbinding site for residue GOL A 505
ChainResidue
AGLU248
ATHR330

site_idAC6
Number of Residues12
Detailsbinding site for residue U5A A 506
ChainResidue
ASER159
APHE165
AILE172
AASN216
AGLN226
ACYS228
AASP239
ATYR255
AASP272
ATYR273
AVAL276
AHOH671

site_idAC7
Number of Residues5
Detailsbinding site for residue FE A 507
ChainResidue
AHIS164
AHIS169
AASP280
AHOH601
AHOH671

site_idAC8
Number of Residues4
Detailsbinding site for residue CL A 508
ChainResidue
ASER41
AHIS42
AASN69
AASN70

site_idAC9
Number of Residues2
Detailsbinding site for residue CL A 509
ChainResidue
AGLN149
AHIS285

site_idAD1
Number of Residues6
Detailsbinding site for residue FES B 501
ChainResidue
BCYS55
BHIS57
BARG58
BCYS74
BHIS77
BTRP79

site_idAD2
Number of Residues3
Detailsbinding site for residue GOL B 502
ChainResidue
BHIS139
BLYS140
BLYS263

site_idAD3
Number of Residues4
Detailsbinding site for residue GOL B 503
ChainResidue
BTHR3
BGLU248
BTHR330
BVAL333

site_idAD4
Number of Residues11
Detailsbinding site for residue U5A B 504
ChainResidue
BSER159
BPHE165
BASN216
BGLN226
BCYS228
BASP239
BTYR255
BASP272
BTYR273
BHOH610
BHOH662

site_idAD5
Number of Residues5
Detailsbinding site for residue FE B 505
ChainResidue
BHIS164
BHIS169
BASP280
BHOH610
BHOH672

site_idAD6
Number of Residues4
Detailsbinding site for residue GOL B 506
ChainResidue
BARG22
BPRO23
BARG40
BASN45

site_idAD7
Number of Residues5
Detailsbinding site for residue GOL B 507
ChainResidue
BTHR143
BLYS144
BTYR146
CGLU19
CASP20

site_idAD8
Number of Residues6
Detailsbinding site for residue FES C 501
ChainResidue
CCYS55
CHIS57
CARG58
CCYS74
CHIS77
CTRP79

site_idAD9
Number of Residues4
Detailsbinding site for residue GOL C 502
ChainResidue
CHIS139
CLYS140
CLYS263
CHOH699

site_idAE1
Number of Residues3
Detailsbinding site for residue GOL C 503
ChainResidue
CLEU305
CGLN307
CCYS334

site_idAE2
Number of Residues5
Detailsbinding site for residue GOL C 504
ChainResidue
AGOL503
AHOH609
CVAL88
CGLN89
CPRO94

site_idAE3
Number of Residues11
Detailsbinding site for residue U5A C 505
ChainResidue
CSER159
CPHE165
CASN216
CGLN226
CCYS228
CASP239
CTYR255
CTYR273
CVAL276
CHOH603
CHOH700

site_idAE4
Number of Residues5
Detailsbinding site for residue FE C 506
ChainResidue
CHIS164
CHIS169
CASP280
CHOH694
CHOH700

site_idAE5
Number of Residues5
Detailsbinding site for residue GOL C 507
ChainResidue
CPRO47
CILE48
CCYS109
CGLN110
CGLU111

site_idAE6
Number of Residues4
Detailsbinding site for residue GOL C 508
ChainResidue
CGLN149
CHIS285
CTHR290
CHOH657

site_idAE7
Number of Residues3
Detailsbinding site for residue GOL C 509
ChainResidue
CGLU248
CARG291
CTHR330

site_idAE8
Number of Residues4
Detailsbinding site for residue CL C 510
ChainResidue
CSER41
CHIS42
CASN69
CASN70

site_idAE9
Number of Residues2
Detailsbinding site for residue CL C 511
ChainResidue
CGLN149
CHIS285

Functional Information from PROSITE/UniProt
site_idPS00570
Number of Residues23
DetailsRING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CpHRGvplsmge.VAnntlvCpYH
ChainResidueDetails
ACYS55-HIS77

224931

PDB entries from 2024-09-11

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