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3OZY

Crystal structure of enolase superfamily member from Bordetella bronchiseptica complexed with Mg and m-Xylarate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0009063biological_processamino acid catabolic process
A0016052biological_processcarbohydrate catabolic process
A0016836molecular_functionhydro-lyase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0009063biological_processamino acid catabolic process
B0016052biological_processcarbohydrate catabolic process
B0016836molecular_functionhydro-lyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 390
ChainResidue
AASP201
AGLU227
AGLU254
AHOH972
AHOH1031
AHOH1032

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 390
ChainResidue
BDXL392
BHOH971
BASP201
BGLU227
BGLU254

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 391
ChainResidue
AHIS86
AHIS90
AHOH1024
BHOH978

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 391
ChainResidue
AHOH976
BHIS86
BHIS90
BHOH734

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE DXL B 392
ChainResidue
BSER25
BLYS30
BTYR147
BLYS171
BLYS173
BASP201
BASN203
BGLU227
BGLU254
BHIS304
BPHE306
BGLU329
BMG390
BHOH531
BHOH971

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 393
ChainResidue
AHIS99
AARG100
AASP264
AHOH405
BARG100
BLEU256
BALA261
BASP264
BHOH498
BHOH588

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 394
ChainResidue
AARG63
AGLU92
BASP57
BGLU378
BPRO379
BHOH521
BHOH525
BHOH615
BHOH623
BHOH763

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 392
ChainResidue
AASP57
AGLU378
AHOH508
AHOH525
AHOH559
AHOH605
BARG63
BASP67
BGLU92
BHOH508

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 393
ChainResidue
AGLU197
AGLY222
ACYS223
APRO247
AARG249
AHOH484
AHOH611
AHOH675

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 395
ChainResidue
AHOH741
BARG22
BHOH571
BHOH820
BHOH868

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY B 396
ChainResidue
BGLY207
BARG208
BHIS298
BHOH483
BHOH487
BHOH540
BHOH850

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 397
ChainResidue
BASP149
BARG176
BASP181
BHOH538
BHOH634

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY A 394
ChainResidue
AGLY207
AARG208
AHIS298
AHOH496
AHOH500
AHOH542
AHOH807
AHOH996

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 395
ChainResidue
AASP181
AHOH447
AHOH581
AASP149
AARG176

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY A 396
ChainResidue
ASER25
AALA27
ALYS30
ATYR147
ALYS173
AASN203
AHOH1035

Functional Information from PROSITE/UniProt
site_idPS00908
Number of Residues26
DetailsMR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AmSGVDiALwDLkGRamnqPIyqLLG
ChainResidueDetails
AALA106-GLY131

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PDB entries from 2024-06-12

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