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6KMN

Crystal Structure of Dye Decolorizing peroxidase from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004325molecular_functionferrochelatase activity
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0016829molecular_functionlyase activity
A0020037molecular_functionheme binding
A0033212biological_processiron import into cell
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
B0004325molecular_functionferrochelatase activity
B0004601molecular_functionperoxidase activity
B0005576cellular_componentextracellular region
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0016829molecular_functionlyase activity
B0020037molecular_functionheme binding
B0033212biological_processiron import into cell
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
C0004325molecular_functionferrochelatase activity
C0004601molecular_functionperoxidase activity
C0005576cellular_componentextracellular region
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0016829molecular_functionlyase activity
C0020037molecular_functionheme binding
C0033212biological_processiron import into cell
C0046872molecular_functionmetal ion binding
C0098869biological_processcellular oxidant detoxification
D0004325molecular_functionferrochelatase activity
D0004601molecular_functionperoxidase activity
D0005576cellular_componentextracellular region
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0016829molecular_functionlyase activity
D0020037molecular_functionheme binding
D0033212biological_processiron import into cell
D0046872molecular_functionmetal ion binding
D0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue HEM A 401
ChainResidue
AASN181
ALYS278
AARG286
ALEU306
APHE308
AMET322
ALEU326
ALEU332
AOXY402
AHOH513
AHOH524
APHE185
AHOH619
ALYS186
AGLY188
ATHR189
AGLY190
AMET227
APHE244
AHIS273

site_idAC2
Number of Residues3
Detailsbinding site for residue OXY A 402
ChainResidue
AASP187
AARG286
AHEM401

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 404
ChainResidue
AMET302
CHOH611

site_idAC4
Number of Residues21
Detailsbinding site for residue HEM B 401
ChainResidue
BASN181
BPHE185
BLYS186
BASP187
BGLY188
BTHR189
BGLY190
BILE225
BMET227
BPHE244
BHIS273
BALA277
BLYS278
BARG286
BLEU306
BPHE308
BPHE319
BMET322
BLEU326
BLEU332
BOXY402

site_idAC5
Number of Residues3
Detailsbinding site for residue OXY B 402
ChainResidue
BASP187
BARG286
BHEM401

site_idAC6
Number of Residues9
Detailsbinding site for residue GOL B 403
ChainResidue
BILE225
BSER327
BASN333
BTHR336
BTHR338
BHOH505
BHOH515
BHOH526
BHOH548

site_idAC7
Number of Residues7
Detailsbinding site for residue MPD B 404
ChainResidue
BALA118
BMET119
BPRO120
DPRO7
DTYR9
DLYS352
DHOH579

site_idAC8
Number of Residues20
Detailsbinding site for residue HEM C 401
ChainResidue
CASN181
CPHE185
CLYS186
CGLY188
CTHR189
CGLY190
CMET227
CPHE244
CARG246
CHIS273
CALA277
CLYS278
CARG286
CLEU306
CPHE308
CMET322
CLEU326
CLEU332
COXY402
CHOH501

site_idAC9
Number of Residues4
Detailsbinding site for residue OXY C 402
ChainResidue
CASP187
CARG286
CPHE308
CHEM401

site_idAD1
Number of Residues18
Detailsbinding site for residue HEM D 401
ChainResidue
DHIS273
DARG286
DLEU306
DPHE308
DLEU326
DLEU332
DOXY402
DHOH521
DASN181
DPHE185
DLYS186
DASP187
DGLY188
DTHR189
DGLY190
DILE225
DMET227
DPHE244

site_idAD2
Number of Residues4
Detailsbinding site for residue OXY D 402
ChainResidue
DASP187
DARG286
DPHE308
DHEM401

site_idAD3
Number of Residues2
Detailsbinding site for residue CL D 403
ChainResidue
DLYS351
DLYS352

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:32971035, ECO:0000269|PubMed:36345957, ECO:0007744|PDB:6KMN, ECO:0007744|PDB:7E5Q
ChainResidueDetails
AGLY188
BGLY188
CGLY188
DGLY188

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: proximal binding residue => ECO:0000269|PubMed:32971035, ECO:0000269|PubMed:36345957, ECO:0007744|PDB:6KMM, ECO:0007744|PDB:6KMN, ECO:0007744|PDB:7E5Q
ChainResidueDetails
AHIS273
BHIS273
CHIS273
DHIS273

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:32971035, ECO:0000269|PubMed:36345957, ECO:0007744|PDB:6KMM, ECO:0007744|PDB:6KMN, ECO:0007744|PDB:7E5Q
ChainResidueDetails
AARG286
BARG286
CARG286
DARG286

223166

PDB entries from 2024-07-31

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