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6WNG

Crystal structure of an aspartate ammonia-lyase from Elizabethkingia anophelis NUHP1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006099biological_processtricarboxylic acid cycle
A0006520biological_processamino acid metabolic process
A0006531biological_processaspartate metabolic process
A0008797molecular_functionaspartate ammonia-lyase activity
A0016829molecular_functionlyase activity
B0003824molecular_functioncatalytic activity
B0006099biological_processtricarboxylic acid cycle
B0006520biological_processamino acid metabolic process
B0006531biological_processaspartate metabolic process
B0008797molecular_functionaspartate ammonia-lyase activity
B0016829molecular_functionlyase activity
C0003824molecular_functioncatalytic activity
C0006099biological_processtricarboxylic acid cycle
C0006520biological_processamino acid metabolic process
C0006531biological_processaspartate metabolic process
C0008797molecular_functionaspartate ammonia-lyase activity
C0016829molecular_functionlyase activity
D0003824molecular_functioncatalytic activity
D0006099biological_processtricarboxylic acid cycle
D0006520biological_processamino acid metabolic process
D0006531biological_processaspartate metabolic process
D0008797molecular_functionaspartate ammonia-lyase activity
D0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue TRS A 501
ChainResidue
AALA308
AHOH734
AHOH768
AHOH926
AASN319
ALEU320
ALYS322
AVAL334
AASN335
APRO336
AHOH603
AHOH673

site_idAC2
Number of Residues13
Detailsbinding site for residue FUM A 502
ChainResidue
AGLY326
ASER327
ASER328
AILE329
AMET330
ALYS333
AASN335
BTHR110
BSER149
BTHR150
BASN151
DTHR196
DGLN197

site_idAC3
Number of Residues9
Detailsbinding site for residue GOL A 503
ChainResidue
AGLU15
ASER16
AVAL32
AGLN33
AGLU118
ATYR135
AHOH767
AHOH901
AHOH932

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 504
ChainResidue
AGLN197
CHOH770
DARG305
DGLU340

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 505
ChainResidue
AARG383
ALYS386
AHOH778

site_idAC6
Number of Residues5
Detailsbinding site for residue CL A 506
ChainResidue
AHIS51
APRO52
AGLU53
AHOH706
AHOH1043

site_idAC7
Number of Residues12
Detailsbinding site for residue TRS B 501
ChainResidue
BALA308
BILE318
BASN319
BLEU320
BVAL334
BASN335
BPRO336
BHOH601
BHOH669
BHOH734
BHOH765
CGLN199

site_idAC8
Number of Residues13
Detailsbinding site for residue FUM B 502
ChainResidue
ATHR110
ASER149
ATHR150
AASN151
BGLY326
BSER327
BSER328
BILE329
BMET330
BLYS333
BASN335
CTHR196
CGLN197

site_idAC9
Number of Residues8
Detailsbinding site for residue GOL B 503
ChainResidue
BSER16
BASP17
BGLN33
BGLU118
BTYR135
BHOH650
BHOH743
BHOH983

site_idAD1
Number of Residues4
Detailsbinding site for residue CL B 504
ChainResidue
BGLN197
CARG305
CGLU340
DHOH655

site_idAD2
Number of Residues3
Detailsbinding site for residue CL B 505
ChainResidue
BARG383
BLYS386
BHOH837

site_idAD3
Number of Residues5
Detailsbinding site for residue CL B 506
ChainResidue
BHIS51
BPRO52
BGLU53
BHOH771
BHOH1047

site_idAD4
Number of Residues12
Detailsbinding site for residue TRS C 601
ChainResidue
CHOH701
CHOH781
CHOH932
CHOH962
BGLN199
CALA308
CILE318
CASN319
CLEU320
CVAL334
CASN335
CPRO336

site_idAD5
Number of Residues13
Detailsbinding site for residue FUM C 602
ChainResidue
BTHR196
BGLN197
CGLY326
CSER327
CSER328
CILE329
CMET330
CLYS333
CASN335
DTHR110
DSER149
DTHR150
DASN151

site_idAD6
Number of Residues9
Detailsbinding site for residue GOL C 603
ChainResidue
CSER16
CASP17
CGLN33
CMET114
CGLU118
CTYR135
CHOH721
CHOH779
CHOH1050

site_idAD7
Number of Residues4
Detailsbinding site for residue CL C 604
ChainResidue
AHOH676
BARG305
BGLU340
CGLN197

site_idAD8
Number of Residues3
Detailsbinding site for residue CL C 605
ChainResidue
CARG383
CLYS386
CHOH934

site_idAD9
Number of Residues5
Detailsbinding site for residue CL C 606
ChainResidue
CHIS51
CPRO52
CGLU53
CHOH832
CHOH1148

site_idAE1
Number of Residues14
Detailsbinding site for residue TRS D 501
ChainResidue
AGLN199
DALA308
DILE318
DASN319
DLEU320
DLYS322
DVAL334
DASN335
DPRO336
DHOH601
DHOH625
DHOH797
DHOH803
DHOH850

site_idAE2
Number of Residues13
Detailsbinding site for residue FUM D 502
ChainResidue
ATHR196
AGLN197
CTHR110
CSER149
CTHR150
CASN151
DGLY326
DSER327
DSER328
DILE329
DMET330
DLYS333
DASN335

site_idAE3
Number of Residues9
Detailsbinding site for residue GOL D 503
ChainResidue
DSER16
DASP17
DGLN33
DMET114
DGLU118
DTYR135
DHOH662
DHOH783
DHOH852

site_idAE4
Number of Residues4
Detailsbinding site for residue CL D 504
ChainResidue
AARG305
AGLU340
BHOH656
DGLN197

site_idAE5
Number of Residues3
Detailsbinding site for residue CL D 505
ChainResidue
DARG383
DLYS386
DHOH840

site_idAE6
Number of Residues5
Detailsbinding site for residue CL D 506
ChainResidue
DHIS51
DPRO52
DGLU53
DHOH787
DHOH1013

Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN
ChainResidueDetails
AGLY326-ASN335

223532

PDB entries from 2024-08-07

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