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5C2I

Crystal structure of Anabaena sp. DyP-type peroxidese (AnaPX)

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
Functional Information from PDB Data
site_idAC1
Number of Residues24
Detailsbinding site for residue HEM A 501
ChainResidue
AGLU198
ATHR335
AASN336
AARG338
AARG365
APHE387
APHE398
AMET401
AGLN402
ALEU421
AILE422
APHE202
AILE449
AHOH706
AHOH716
AHOH730
AHOH814
AVAL203
AHIS204
AGLY205
AVAL206
ASER207
AGLN262
AHIS331

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 502
ChainResidue
AGLU184
ALYS259
ATYR370
AGLY371
AGLY382
AHOH649
AHOH807
BGLN165

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 503
ChainResidue
ASER237
AGLY360
ASER392
AASN393
AASN396
AGLN397

site_idAC4
Number of Residues25
Detailsbinding site for residue HEM B 501
ChainResidue
BGLU198
BPHE202
BVAL203
BHIS204
BGLY205
BVAL206
BSER207
BGLN262
BVAL290
BHIS331
BTHR335
BASN336
BARG338
BARG365
BPHE387
BPHE398
BMET401
BGLN402
BLEU421
BILE422
BILE449
BHOH608
BHOH619
BHOH670
BHOH675

site_idAC5
Number of Residues11
Detailsbinding site for residue GOL B 502
ChainResidue
AGLN165
AASN168
AGLN169
AHOH607
BGLU184
BLYS259
BTYR370
BGLY371
BGLY382
BHOH611
BHOH755

site_idAC6
Number of Residues25
Detailsbinding site for residue HEM C 501
ChainResidue
CGLU198
CPHE202
CVAL203
CHIS204
CGLY205
CVAL206
CSER207
CGLN262
CVAL290
CHIS331
CTHR335
CASN336
CARG338
CARG365
CPHE387
CPHE398
CMET401
CGLN402
CLEU421
CILE422
CILE449
CHOH641
CHOH644
CHOH651
CHOH691

site_idAC7
Number of Residues10
Detailsbinding site for residue GOL C 502
ChainResidue
CGLU184
CLYS259
CTYR370
CGLY371
CGLY382
CHOH630
CHOH640
CHOH780
DGLN165
DGLN169

site_idAC8
Number of Residues6
Detailsbinding site for residue ACY C 503
ChainResidue
AGLN64
ATHR467
AALA469
CLYS118
CPRO119
CGLU395

site_idAC9
Number of Residues6
Detailsbinding site for residue EDO C 504
ChainResidue
CSER237
CGLY360
CSER392
CASN393
CASN396
CGLN397

site_idAD1
Number of Residues24
Detailsbinding site for residue HEM D 501
ChainResidue
DGLU198
DPHE202
DVAL203
DHIS204
DGLY205
DVAL206
DSER207
DGLN262
DHIS331
DTHR335
DASN336
DARG338
DARG365
DPHE387
DPHE398
DMET401
DGLN402
DLEU421
DILE422
DILE449
DHOH621
DHOH700
DHOH702
DHOH749

site_idAD2
Number of Residues8
Detailsbinding site for residue GOL D 502
ChainResidue
CGLN165
CGLN169
DGLU184
DLYS259
DTYR370
DGLY371
DGLY382
DHOH616

site_idAD3
Number of Residues10
Detailsbinding site for residue GOL D 503
ChainResidue
ALYS273
ATYR443
AASN444
DASN20
DPRO21
DGLY22
DARG25
DHOH625
DHOH699
DHOH701

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PDB entries from 2024-11-06

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