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5MA2

PCE reductive dehalogenase from S. multivorans in complex with 4-iodophenol

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SF4 A 501
ChainResidue
AMET292
ACYS329
ACYS332
ALYS333
ACYS335
ACYS390

site_idAC2
Number of Residues8
Detailsbinding site for residue SF4 A 502
ChainResidue
ACYS372
ACYS383
AGLY384
ACYS386
ABVQ503
ACYS339
APRO340
ASER341

site_idAC3
Number of Residues40
Detailsbinding site for residue BVQ A 503
ChainResidue
ATYR31
ATHR36
AALA37
APHE38
ATYR170
ATHR242
ATYR246
AMET249
AASN272
AGLY275
AGLN276
ASER277
AVAL278
AALA289
AMET292
AGLY293
AALA294
ACYS295
APRO302
AVAL304
AARG305
ALEU306
ALYS308
AHIS357
AASN358
AGLN359
ALYS362
AGLN364
ATYR369
ACYS372
ATRP376
ATYR382
AVAL387
ASF4502
AHOH602
AHOH625
AHOH721
AHOH734
AHOH767
AHOH843

site_idAC4
Number of Residues4
Detailsbinding site for residue BEN A 504
ChainResidue
ATHR39
APHE44
AGLU189
AILE399

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 505
ChainResidue
APHE38
AASN101
AGLU189
AHOH606
AHOH670

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 506
ChainResidue
APHE110
ALEU113
AMET119
AHOH631
AHOH643
AHOH780
BPHE111

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL A 508
ChainResidue
AARG349
APHE351
AHOH601
AHOH605
BGLU172

site_idAC8
Number of Residues9
Detailsbinding site for residue IOL A 509
ChainResidue
APHE38
ATRP56
ATRP96
ATYR102
ATYR246
AARG305
ATRP376
ATYR382
AHOH602

site_idAC9
Number of Residues2
Detailsbinding site for residue IOL A 510
ChainResidue
AILE399
AHOH862

site_idAD1
Number of Residues4
Detailsbinding site for residue IOL A 511
ChainResidue
ALEU58
ALEU186
AHIS187
BLEU124

site_idAD2
Number of Residues4
Detailsbinding site for residue IOD A 512
ChainResidue
AALA60
ALYS64
AGLY381
ATYR382

site_idAD3
Number of Residues9
Detailsbinding site for residue SF4 B 501
ChainResidue
BLYS333
BCYS335
BCYS390
BPHE392
BARG291
BMET292
BPHE328
BCYS329
BCYS332

site_idAD4
Number of Residues8
Detailsbinding site for residue SF4 B 502
ChainResidue
BCYS339
BPRO340
BSER341
BCYS372
BCYS383
BGLY384
BCYS386
BBVQ503

site_idAD5
Number of Residues40
Detailsbinding site for residue BVQ B 503
ChainResidue
BTYR31
BTHR36
BALA37
BPHE38
BTYR170
BTHR242
BTYR246
BMET249
BASN272
BGLY275
BGLN276
BSER277
BVAL278
BALA289
BMET292
BGLY293
BALA294
BCYS295
BPRO302
BVAL304
BARG305
BLEU306
BLYS308
BHIS357
BASN358
BGLN359
BLYS362
BGLN364
BTYR369
BCYS372
BTRP376
BTYR382
BVAL387
BSF4502
BHOH617
BHOH624
BHOH661
BHOH703
BHOH784
BHOH822

site_idAD6
Number of Residues6
Detailsbinding site for residue GOL B 504
ChainResidue
BTRP56
BPHE57
BLEU186
BGLU189
BHOH607
BHOH621

site_idAD7
Number of Residues7
Detailsbinding site for residue GOL B 505
ChainResidue
APHE111
BPHE110
BLEU113
BMET119
BHOH610
BHOH629
BHOH733

site_idAD8
Number of Residues3
Detailsbinding site for residue IOL B 507
ChainResidue
AASP322
BPHE45
BHOH602

site_idAD9
Number of Residues3
Detailsbinding site for residue IOL B 508
ChainResidue
ALEU124
BLEU186
BHIS187

site_idAE1
Number of Residues7
Detailsbinding site for residue IOL B 509
ChainResidue
BPHE38
BTRP56
BTYR102
BTYR246
BARG305
BTRP376
BTYR382

site_idAE2
Number of Residues3
Detailsbinding site for residue IOD B 511
ChainResidue
BALA60
BLYS64
BTYR382

site_idAE3
Number of Residues16
Detailsbinding site for residues GOL A 507 and IOL B 506
ChainResidue
APHE110
ALEU113
AMET119
AASP322
AGLU327
AGLU330
APRO348
AARG349
AHOH631
AHOH643
AHOH679
AHOH780
BPRO41
BPHE45
BPHE111
BHOH602

Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CeTCKkCArECP
ChainResidueDetails
ACYS329-PRO340

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsBINDING: BINDING => ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G, ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W, ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP
ChainResidueDetails
AALA37
AHIS357
ACYS372
ATYR382
ACYS383
ACYS386
ACYS390
BALA37
BTYR170
BASN272
BMET292
ATYR170
BVAL304
BCYS329
BCYS332
BCYS335
BCYS339
BHIS357
BCYS372
BTYR382
BCYS383
BCYS386
AASN272
BCYS390
AMET292
AVAL304
ACYS329
ACYS332
ACYS335
ACYS339

223532

PDB entries from 2024-08-07

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