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4UR3

Crystal structure of the PCE reductive dehalogenase from S. multivorans P2(1) crystal form

Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 A 501
ChainResidue
ASER290
AARG291
ACYS329
ACYS332
ACYS335
ACYS390

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 A 502
ChainResidue
ACYS383
AGLY384
ACYS386
ABVQ503
ACYS339
ASER341
ACYS372

site_idAC3
Number of Residues34
DetailsBINDING SITE FOR RESIDUE BVQ A 503
ChainResidue
ATYR31
ATHR36
AALA37
APHE38
ATYR170
ATYR246
AMET249
AASN272
AGLY275
AGLN276
ASER277
AVAL278
AALA289
AMET292
AGLY293
AALA294
ACYS295
AVAL304
AARG305
ALEU306
AHIS357
AASN358
AGLN359
ALYS362
AGLN364
ATYR369
ACYS372
ATRP376
ATYR382
ASF4502
AHOH2132
AHOH2135
AHOH2163
AHOH2191

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 B 501
ChainResidue
BMET292
BCYS329
BCYS332
BCYS335
BCYS390
BPHE392

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 B 502
ChainResidue
BCYS339
BSER341
BILE344
BCYS372
BCYS383
BGLY384
BCYS386
BBVQ503

site_idAC6
Number of Residues37
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
BHIS357
BASN358
BGLN359
BLYS362
BGLN364
BTYR369
BCYS372
BTRP376
BTYR382
BSF4502
BHOH2135
BHOH2137
BHOH2175
BHOH2176
BHOH2196

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 C 501
ChainResidue
CCYS329
CCYS332
CLYS333
CCYS335
CCYS390
CMET292

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 C 502
ChainResidue
CCYS339
CPRO340
CSER341
CCYS372
CCYS383
CGLY384
CCYS386
CBVQ503

site_idAC9
Number of Residues35
DetailsBINDING SITE FOR RESIDUE BVQ C 503
ChainResidue
CTYR31
CTHR36
CALA37
CPHE38
CTYR170
CTHR242
CMET249
CASN272
CGLY275
CGLN276
CSER277
CVAL278
CALA289
CMET292
CGLY293
CALA294
CCYS295
CPRO302
CVAL304
CARG305
CLEU306
CLYS308
CHIS357
CASN358
CGLN359
CLYS362
CGLN364
CTYR369
CCYS372
CTRP376
CTYR382
CSF4502
CHOH2179
CHOH2180
CHOH2252

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 D 501
ChainResidue
DSER290
DARG291
DMET292
DPHE328
DCYS329
DCYS332
DCYS335
DCYS390
DPHE392

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 D 502
ChainResidue
DCYS339
DPRO340
DSER341
DCYS372
DCYS383
DGLY384
DCYS386
DBVQ503

site_idBC3
Number of Residues38
DetailsBINDING SITE FOR RESIDUE BVQ D 503
ChainResidue
DTYR31
DTHR36
DALA37
DPHE38
DTYR170
DTHR242
DMET249
DASN272
DGLY275
DGLN276
DSER277
DVAL278
DALA289
DMET292
DGLY293
DALA294
DCYS295
DPRO302
DVAL304
DARG305
DLEU306
DLYS308
DHIS357
DASN358
DGLN359
DLYS362
DGLN364
DTYR369
DCYS372
DTRP376
DTYR382
DSF4502
DHOH2134
DHOH2138
DHOH2139
DHOH2168
DHOH2170
DHOH2197

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 E 501
ChainResidue
EARG291
EMET292
ECYS329
ECYS332
ECYS335
ECYS390
EPRO391

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 E 502
ChainResidue
ECYS339
ESER341
ECYS372
ECYS383
EGLY384
EVAL385
ECYS386
EBVQ503

site_idBC6
Number of Residues34
DetailsBINDING SITE FOR RESIDUE BVQ E 503
ChainResidue
ETHR36
EALA37
EPHE38
ETYR170
ETYR246
EMET249
EASN272
EGLY275
EGLN276
ESER277
EVAL278
EALA289
EMET292
EGLY293
EALA294
ECYS295
EPRO302
EVAL304
EARG305
ELEU306
EHIS357
EASN358
EGLN359
ELYS362
EGLN364
ETYR369
ECYS372
ETRP376
ETYR382
ECYS386
EVAL387
ESF4502
EHOH2080
EHOH2098

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 F 501
ChainResidue
FARG291
FMET292
FPHE328
FCYS329
FCYS332
FCYS335
FCYS390
FPRO391

site_idBC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 F 502
ChainResidue
FCYS339
FPRO340
FSER341
FCYS372
FCYS383
FGLY384
FVAL385
FCYS386
FBVQ503

site_idBC9
Number of Residues37
DetailsBINDING SITE FOR RESIDUE BVQ F 503
ChainResidue
FILE22
FTYR31
FTHR36
FALA37
FPHE38
FTYR170
FTHR242
FMET249
FASN272
FGLY275
FGLN276
FSER277
FVAL278
FALA279
FALA289
FMET292
FGLY293
FALA294
FCYS295
FVAL304
FARG305
FLEU306
FHIS357
FASN358
FGLN359
FLYS362
FGLN364
FTYR369
FCYS372
FTRP376
FTYR382
FSF4502
FHOH2096
FHOH2099
FHOH2100
FHOH2121
FHOH2132

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

223790

PDB entries from 2024-08-14

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