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1H21

A novel iron centre in the split-Soret cytochrome c from Desulfovibrio desulfuricans ATCC 27774

Replaces:  1DDC
Functional Information from GO Data
ChainGOidnamespacecontents
A0009061biological_processanaerobic respiration
A0046872molecular_functionmetal ion binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0009061biological_processanaerobic respiration
B0046872molecular_functionmetal ion binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
C0009061biological_processanaerobic respiration
C0046872molecular_functionmetal ion binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
D0009061biological_processanaerobic respiration
D0046872molecular_functionmetal ion binding
D0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HEC A1248
ChainResidue
ASER208
BHIS246
BPRO247
ACYS209
ACYS212
AHIS213
ATRP222
AHIS233
AHEC1249
BLYS242
BPHE243

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEC A1249
ChainResidue
ACYS209
AHIS213
AGLY225
AMET227
AASP228
ACYS229
ACYS232
AHIS233
AHEC1248
BHIS148
BILE149
BSER152
BLYS153
BTYR156
BPRO231
BALA238
BHEC1249

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEC B1248
ChainResidue
ATYR156
AALA237
AALA238
ALYS242
AHIS246
APRO247
BCYS209
BCYS212
BHIS213
BALA220
BHIS233
BHEC1249

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEC B1249
ChainResidue
AHIS148
AILE149
ASER152
ALYS153
ATYR156
AALA238
AHEC1249
BCYS209
BHIS213
BMET214
BGLY225
BMET227
BASP228
BCYS229
BCYS232
BHIS233
BHEC1248

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEC C1248
ChainResidue
CCYS209
CHIS213
CMET214
CGLY225
CMET227
CASP228
CCYS229
CCYS232
CHIS233
DHIS148
DILE149
DSER152
DLYS153
DTYR156
DPRO231
DALA238
DHEC1248
DHEC1250

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEC D1248
ChainResidue
BLYS23
BLEU24
BASP25
CCYS209
CCYS212
CHIS213
CALA220
CHIS233
CHEC1248
DTYR156
DALA237
DALA238
DLYS242
DPHE243
DHIS246
DPRO247
DHOH2052
DHOH2053

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEC D1249
ChainResidue
CPRO247
DSER208
DCYS209
DCYS212
DHIS213
DTRP222
DHIS233
DHEC1250
CTYR156
CALA237
CALA238
CLYS242
CPHE243
CHIS246

site_idAC8
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEC D1250
ChainResidue
CHIS148
CILE149
CSER152
CLYS153
CTYR156
CPRO231
CALA238
CHEC1248
DCYS209
DHIS213
DGLY225
DMET227
DASP228
DCYS229
DCYS232
DHIS233
DHEC1249

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALYS76
CVAL118
CALA179
CGLN203
DLYS76
DVAL118
DALA179
DGLN203
AVAL118
AALA179
AGLN203
BLYS76
BVAL118
BALA179
BGLN203
CLYS76

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: axial binding residue; in chain B => ECO:0000269|PubMed:12589573, ECO:0007744|PDB:1H21
ChainResidueDetails
APHE180
BPHE180
CPHE180
DPHE180

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: covalent; in chain A => ECO:0000269|PubMed:12589573, ECO:0007744|PDB:1H21
ChainResidueDetails
AASN241
AVAL244
BASN241
BVAL244
CASN241
CVAL244
DASN241
DVAL244

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: axial binding residue; in chain A => ECO:0000269|PubMed:12589573, ECO:0007744|PDB:1H21
ChainResidueDetails
AASN245
BASN245
CASN245
DASN245

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Blocked amino end (Gly)
ChainResidueDetails
AALA33
BALA33
CALA33
DALA33

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PDB entries from 2024-11-06

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