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6CZ9

The arsenate respiratory reductase (Arr) complex from Shewanella sp. ANA-3 bound to arsenite

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0042597cellular_componentperiplasmic space
A0043546molecular_functionmolybdopterin cofactor binding
A0046872molecular_functionmetal ion binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
C0016491molecular_functionoxidoreductase activity
C0042597cellular_componentperiplasmic space
C0043546molecular_functionmolybdopterin cofactor binding
C0046872molecular_functionmetal ion binding
C0051539molecular_function4 iron, 4 sulfur cluster binding
D0042597cellular_componentperiplasmic space
D0046872molecular_functionmetal ion binding
D0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue SF4 A 901
ChainResidue
ACYS61
AARG98
ASER236
AGLY63
ACYS64
ASER66
ATRP67
ACYS68
ALYS70
ASER95
ACYS96

site_idAC2
Number of Residues35
Detailsbinding site for residue MGD A 902
ChainResidue
ACYS64
AARG98
AARG165
ACYS193
APHE224
AGLY225
AALA230
ASER231
AASN232
AVAL254
AASP255
APRO256
AARG257
APRO273
AGLY274
AASP276
ASER373
AARG374
AGLY375
AGLN379
AVAL721
AASP722
ALYS724
ASER725
AARG726
AASN728
AGLU730
ATYR844
AMGD903
AMO904
AAST905
AHOH1075
AHOH1155
AHOH1264
AHOH1294

site_idAC3
Number of Residues36
Detailsbinding site for residue MGD A 903
ChainResidue
AGLY164
AARG165
AHIS189
AVAL192
ACYS193
AARG374
APHE481
AASN482
AASN483
APHE484
ASER487
AILE507
ATHR508
ATHR509
ASER512
ASER524
AHIS526
AHIS527
AASP561
AASP722
ALYS724
AGLU730
AGLY731
AARG732
APHE802
ATYR809
AASN827
APHE843
AMGD902
AMO904
AAST905
AHOH1050
AHOH1061
AHOH1100
AHOH1111
AHOH1284

site_idAC4
Number of Residues4
Detailsbinding site for residue MO A 904
ChainResidue
ACYS193
AMGD902
AMGD903
AAST905

site_idAC5
Number of Residues10
Detailsbinding site for residue AST A 905
ChainResidue
AARG165
ATYR166
AHIS189
ACYS193
ATYR210
AMGD902
AMGD903
AMO904
AHOH1051
AHOH1330

site_idAC6
Number of Residues5
Detailsbinding site for residue FMT A 906
ChainResidue
AHOH1229
AHOH1426
ATYR645
ALYS646
AALA649

site_idAC7
Number of Residues7
Detailsbinding site for residue FMT A 907
ChainResidue
AGLN62
AGLY63
AGLN105
AHIS527
ALYS729
AARG732
AHOH1050

site_idAC8
Number of Residues3
Detailsbinding site for residue FMT A 908
ChainResidue
AARG50
AASP76
BGLU215

site_idAC9
Number of Residues7
Detailsbinding site for residue FMT A 909
ChainResidue
AGLU753
AASP754
AGLY823
AHOH1104
AHOH1269
DASN97
DHOH447

site_idAD1
Number of Residues3
Detailsbinding site for residue PG5 A 910
ChainResidue
AARG794
APRO795
AHOH1005

site_idAD2
Number of Residues8
Detailsbinding site for residue SF4 B 301
ChainResidue
BCYS12
BVAL13
BCYS15
BGLY16
BCYS18
BTYR52
BCYS183
BARG188

site_idAD3
Number of Residues10
Detailsbinding site for residue SF4 B 302
ChainResidue
BCYS22
BASN26
BTRP34
BSER35
BCYS164
BTHR165
BPHE166
BCYS167
BPRO177
BCYS179

site_idAD4
Number of Residues10
Detailsbinding site for residue SF4 B 303
ChainResidue
BCYS57
BASN58
BCYS60
BPRO64
BCYS65
BTHR82
BCYS99
BTYR101
BILE104
BLYS163

site_idAD5
Number of Residues9
Detailsbinding site for residue SF4 B 304
ChainResidue
BCYS69
BTHR71
BGLN84
BCYS89
BILE90
BCYS92
BLYS93
BCYS95
BTHR161

site_idAD6
Number of Residues4
Detailsbinding site for residue FMT B 305
ChainResidue
BARG2
BLEU193
BHOH411
BHOH448

site_idAD7
Number of Residues12
Detailsbinding site for residue SF4 C 901
ChainResidue
CCYS61
CGLY63
CCYS64
CSER66
CTRP67
CCYS68
CLYS70
CSER95
CCYS96
CARG98
CVAL235
CSER236

site_idAD8
Number of Residues37
Detailsbinding site for residue MGD C 902
ChainResidue
CCYS64
CTHR65
CARG98
CARG165
CCYS193
CPHE224
CGLY225
CALA230
CSER231
CASN232
CVAL254
CASP255
CPRO256
CARG257
CPRO273
CGLY274
CASP276
CSER373
CARG374
CGLY375
CGLN379
CVAL721
CASP722
CLYS724
CSER725
CARG726
CASN728
CGLU730
CTYR844
CMGD903
CMO904
CAST905
CHOH1087
CHOH1098
CHOH1189
CHOH1201
CHOH1480

site_idAD9
Number of Residues36
Detailsbinding site for residue MGD C 903
ChainResidue
CGLY164
CARG165
CHIS189
CVAL192
CCYS193
CARG374
CPHE481
CASN482
CASN483
CPHE484
CSER487
CILE507
CTHR508
CTHR509
CSER512
CSER524
CHIS527
CASP561
CASP722
CLYS724
CGLU730
CGLY731
CARG732
CPHE802
CTYR809
CASN827
CPHE843
CMGD902
CMO904
CAST905
CHOH1156
CHOH1183
CHOH1308
CHOH1310
CHOH1316
CHOH1497

site_idAE1
Number of Residues4
Detailsbinding site for residue MO C 904
ChainResidue
CCYS193
CMGD902
CMGD903
CAST905

site_idAE2
Number of Residues12
Detailsbinding site for residue AST C 905
ChainResidue
CTHR65
CARG165
CTYR166
CHIS189
CCYS193
CTYR210
CMGD902
CMGD903
CMO904
CHOH1041
CHOH1146
CHOH1594

site_idAE3
Number of Residues6
Detailsbinding site for residue FMT C 906
ChainResidue
CPRO737
CTYR740
CARG822
CHOH1076
CHOH1171
CHOH1623

site_idAE4
Number of Residues5
Detailsbinding site for residue FMT C 907
ChainResidue
CGLN105
CHIS527
CLYS729
CARG732
CHOH1037

site_idAE5
Number of Residues6
Detailsbinding site for residue FMT C 908
ChainResidue
CTYR645
CLYS646
CALA649
CHOH1094
CHOH1282
CHOH1335

site_idAE6
Number of Residues4
Detailsbinding site for residue PG5 C 909
ChainResidue
CGLU272
CILE346
CARG794
CPRO795

site_idAE7
Number of Residues8
Detailsbinding site for residue SF4 D 301
ChainResidue
DCYS12
DVAL13
DCYS15
DGLY16
DCYS18
DTYR52
DCYS183
DARG188

site_idAE8
Number of Residues10
Detailsbinding site for residue SF4 D 302
ChainResidue
DCYS22
DASN26
DTRP34
DSER35
DCYS164
DTHR165
DPHE166
DCYS167
DPRO177
DCYS179

site_idAE9
Number of Residues10
Detailsbinding site for residue SF4 D 303
ChainResidue
DCYS57
DASN58
DCYS60
DPRO64
DCYS65
DTHR82
DCYS99
DTYR101
DILE104
DLYS163

site_idAF1
Number of Residues9
Detailsbinding site for residue SF4 D 304
ChainResidue
DCYS69
DTHR71
DGLN84
DCYS89
DILE90
DCYS92
DLYS93
DCYS95
DTHR161

site_idAF2
Number of Residues4
Detailsbinding site for residue PEG D 305
ChainResidue
BARG113
DPRO70
DHOH403
DHOH589

Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiGCKkCMnACP
ChainResidueDetails
BCYS89-PRO100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:30104376, ECO:0007744|PDB:6CZ7, ECO:0007744|PDB:6CZ8, ECO:0007744|PDB:6CZ9, ECO:0007744|PDB:6CZA
ChainResidueDetails
BCYS12
BCYS15
BCYS18
BCYS22
BCYS57
BCYS60
BCYS65
BCYS69
BCYS89
BCYS92
BCYS95
BCYS99
BCYS164
BCYS167
BCYS179
BCYS183
DCYS12
DCYS15
DCYS18
DCYS22
DCYS57
DCYS60
DCYS65
DCYS69
DCYS89
DCYS92
DCYS95
DCYS99
DCYS164
DCYS167
DCYS179
DCYS183

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:30104376, ECO:0007744|PDB:6CZ9
ChainResidueDetails
AARG165
AHIS189
ATYR210
CARG165
CHIS189
CTYR210

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:30104376, ECO:0007744|PDB:6CZ8
ChainResidueDetails
ATYR166
ASER190
ALYS198
CTYR166
CSER190
CLYS198

219869

PDB entries from 2024-05-15

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