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4RDY

Crystal structure of VmoLac bound to 3-oxo-C10 AHL

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0009056biological_processcatabolic process
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0046872molecular_functionmetal ion binding
B0008270molecular_functionzinc ion binding
B0009056biological_processcatabolic process
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO A 401
ChainResidue
AHIS23
AHIS25
AKCX138
AASP257
ACO402
A3M5403
AHOH830

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO A 402
ChainResidue
AHIS200
AARG224
ACO401
A3M5403
AHOH830
AKCX138
AHIS171

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 3M5 A 403
ChainResidue
AHIS25
ALEU28
ATYR98
AKCX138
AHIS171
AARG224
AASP257
AILE262
ATRP264
ATRP277
ACO401
ACO402
AHOH830

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
AALA53
ATYR258
ATHR278
AMET279
AHOH554

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 405
ChainResidue
ALEU146
AARG155
AASP181
AARG184
AGLU188

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 406
ChainResidue
ATHR99
ATYR100
ATRP264
AHOH524
AHOH543
AHOH616
BPHE105

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 407
ChainResidue
ALEU180
AARG184
ALYS187
AGLU216
AHOH709
AHOH727

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 408
ChainResidue
AARG110
AHOH561
AHOH585
AHOH738
AHOH795
BPRO266
BGOL406

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 409
ChainResidue
AALA194
AGLY217
APHE219
AASP250
AGLN251
AARG310
AHOH640

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 410
ChainResidue
ALEU40
ATYR41
AILE262
AASP263
ATYR265
APRO267
ASO4412
AHOH695
AHOH698
BARG110
BHOH598

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 411
ChainResidue
AARG34
APRO38
AHOH570
AHOH685
AHOH789

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 412
ChainResidue
APRO267
AGLU268
AGOL410
BARG110
BHOH598

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO B 401
ChainResidue
BHIS23
BHIS25
BKCX138
BASP257
BCO402
B3M5403
BHOH829

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO B 402
ChainResidue
BKCX138
BHIS171
BHIS200
BARG224
BCO401
B3M5403
BHOH829

site_idBC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 3M5 B 403
ChainResidue
BHIS25
BLEU28
BTYR98
BKCX138
BHIS171
BARG224
BTYR230
BASP257
BILE262
BTRP264
BTYR265
BVAL269
BTHR273
BTRP277
BCO401
BCO402
BHOH829

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 404
ChainResidue
BGLY217
BALA218
BPHE219
BASP250
BARG310
BHOH708
BHOH712
BHOH795

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 405
ChainResidue
BALA53
BTHR278
BMET279
BHOH560
BHOH631

site_idBC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL B 406
ChainResidue
AARG110
AGOL408
AHOH561
BLEU40
BTYR41
BTHR261
BILE262
BASP263
BTYR265
BPRO267
BHOH556
BHOH630

site_idCC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 407
ChainResidue
BARG49
BTYR258
BCYS259
BPRO260
BPRO267
BHOH625
BHOH630
BHOH709
BHOH760

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 408
ChainResidue
BASP250
BARG302
BHOH576

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 409
ChainResidue
BVAL174
BTHR204
BASP206
BPHE209

Functional Information from PROSITE/UniProt
site_idPS01322
Number of Residues9
DetailsPHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GlTLfHEHL
ChainResidueDetails
AGLY18-LEU26

223532

PDB entries from 2024-08-07

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