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6QZO

Crystal structure of DyP-type peroxidase from Cellulomonas bogoriensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005829cellular_componentcytosol
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
B0004601molecular_functionperoxidase activity
B0005829cellular_componentcytosol
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
C0004601molecular_functionperoxidase activity
C0005829cellular_componentcytosol
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
C0098869biological_processcellular oxidant detoxification
D0004601molecular_functionperoxidase activity
D0005829cellular_componentcytosol
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
D0098869biological_processcellular oxidant detoxification
E0004601molecular_functionperoxidase activity
E0005829cellular_componentcytosol
E0020037molecular_functionheme binding
E0046872molecular_functionmetal ion binding
E0098869biological_processcellular oxidant detoxification
F0004601molecular_functionperoxidase activity
F0005829cellular_componentcytosol
F0020037molecular_functionheme binding
F0046872molecular_functionmetal ion binding
F0098869biological_processcellular oxidant detoxification
G0004601molecular_functionperoxidase activity
G0005829cellular_componentcytosol
G0020037molecular_functionheme binding
G0046872molecular_functionmetal ion binding
G0098869biological_processcellular oxidant detoxification
H0004601molecular_functionperoxidase activity
H0005829cellular_componentcytosol
H0020037molecular_functionheme binding
H0046872molecular_functionmetal ion binding
H0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue HEM A 401
ChainResidue
AASN195
AALA296
APHE305
AARG307
APHE328
APHE339
AVAL342
AGLN343
ALEU352
ATHR356
AGLN199
AVAL200
AGLU201
AGLY202
ATHR203
AALA204
AILE236
AHIS292

site_idAC2
Number of Residues20
Detailsbinding site for residue HEM B 401
ChainResidue
BASN195
BGLN199
BVAL200
BGLU201
BGLY202
BTHR203
BALA204
BILE236
BHIS292
BALA296
BPHE305
BARG307
BPHE328
BPHE339
BVAL342
BGLN343
BLEU346
BLEU352
BTHR356
BHOH507

site_idAC3
Number of Residues20
Detailsbinding site for residue HEM C 401
ChainResidue
CASN195
CGLN199
CVAL200
CGLU201
CGLY202
CTHR203
CALA204
CILE236
CHIS292
CALA296
CARG297
CPHE305
CARG307
CPHE328
CVAL342
CGLN343
CLEU346
CLEU352
CTHR356
CHOH524

site_idAC4
Number of Residues17
Detailsbinding site for residue HEM D 401
ChainResidue
DASN195
DGLN199
DVAL200
DGLU201
DGLY202
DTHR203
DALA204
DILE236
DHIS292
DALA296
DPHE305
DARG307
DPHE328
DVAL342
DLEU346
DLEU352
DTHR356

site_idAC5
Number of Residues20
Detailsbinding site for residue HEM E 401
ChainResidue
EGLN199
EVAL200
EGLU201
EGLY202
ETHR203
EALA204
EILE236
EARG257
EHIS292
EALA296
EARG297
EPRO298
EPHE305
EARG307
EPHE328
EVAL342
EGLN343
ELEU352
ETHR356
EHOH505

site_idAC6
Number of Residues20
Detailsbinding site for residue HEM F 401
ChainResidue
FGLY202
FTHR203
FALA204
FILE236
FHIS292
FALA296
FARG297
FPRO298
FPHE305
FARG307
FLEU326
FPHE328
FVAL342
FGLN343
FLEU346
FTHR356
FASN195
FGLN199
FVAL200
FGLU201

site_idAC7
Number of Residues21
Detailsbinding site for residue HEM G 401
ChainResidue
GASN195
GGLN199
GVAL200
GGLU201
GGLY202
GTHR203
GALA204
GILE236
GARG257
GHIS292
GILE293
GALA296
GARG297
GPRO298
GPHE305
GARG307
GPHE328
GVAL342
GGLN343
GLEU352
GTHR356

site_idAC8
Number of Residues22
Detailsbinding site for residue HEM H 401
ChainResidue
HASN195
HGLN199
HVAL200
HGLU201
HGLY202
HTHR203
HALA204
HILE236
HARG257
HHIS292
HALA296
HARG297
HPRO298
HPHE305
HARG307
HLEU326
HPHE328
HVAL342
HGLN343
HLEU346
HTHR356
HHOH506

site_idAC9
Number of Residues4
Detailsbinding site for residue PGE H 402
ChainResidue
HALA250
HTHR254
HASP288
HLEU351

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PDB entries from 2024-08-14

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