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5X8G

Binary complex structure of a double mutant I454RA456K of o-Succinylbenzoate CoA Synthetase (MenE) from Bacillus Subtilis bound with its product analogue OSB-NCoA at 1.90 angstrom

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0008756molecular_functiono-succinylbenzoate-CoA ligase activity
A0009234biological_processmenaquinone biosynthetic process
A0016405molecular_functionCoA-ligase activity
A0016874molecular_functionligase activity
B0005524molecular_functionATP binding
B0008756molecular_functiono-succinylbenzoate-CoA ligase activity
B0009234biological_processmenaquinone biosynthetic process
B0016405molecular_functionCoA-ligase activity
B0016874molecular_functionligase activity
C0005524molecular_functionATP binding
C0008756molecular_functiono-succinylbenzoate-CoA ligase activity
C0009234biological_processmenaquinone biosynthetic process
C0016405molecular_functionCoA-ligase activity
C0016874molecular_functionligase activity
D0005524molecular_functionATP binding
D0008756molecular_functiono-succinylbenzoate-CoA ligase activity
D0009234biological_processmenaquinone biosynthetic process
D0016405molecular_functionCoA-ligase activity
D0016874molecular_functionligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues40
Detailsbinding site for residue S0N A 501
ChainResidue
ALYS86
AGLY264
AGLY287
ASER293
AGLN294
ASER389
AGLY390
AGLY391
AGLU392
ALYS421
ATRP422
APRO193
ATYR452
AMG502
ACA505
AHOH625
AHOH638
AHOH659
AHOH678
AHOH706
AHOH712
AHOH720
AILE197
AHOH749
AHOH761
AHOH787
AHOH810
AHOH871
AHOH881
AHOH893
AHOH917
DSER220
DVAL221
ASER198
DSER222
AARG218
APHE219
AALA238
ALEU261
AGLY263

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 502
ChainResidue
APHE219
AS0N501
AHOH881
AHOH912
AHOH946

site_idAC3
Number of Residues3
Detailsbinding site for residue MG A 503
ChainResidue
AASN7
AHIS71
APHE74

site_idAC4
Number of Residues4
Detailsbinding site for residue CA A 505
ChainResidue
AHIS196
AILE197
ATHR289
AS0N501

site_idAC5
Number of Residues2
Detailsbinding site for residue CA A 506
ChainResidue
AGLU355
APHE358

site_idAC6
Number of Residues2
Detailsbinding site for residue NA A 507
ChainResidue
AHOH751
AHOH839

site_idAC7
Number of Residues7
Detailsbinding site for residue PEG A 508
ChainResidue
ALEU180
AGLY181
AHOH612
AHOH764
CILE182
CTHR183
CGLU184

site_idAC8
Number of Residues1
Detailsbinding site for residue PEG A 509
ChainResidue
AGLY366

site_idAC9
Number of Residues4
Detailsbinding site for residue PEG A 510
ChainResidue
AGLN14
APHE35
AHOH656
AHOH679

site_idAD1
Number of Residues39
Detailsbinding site for residue S0N B 501
ChainResidue
BHOH718
BHOH799
BHOH814
BHOH872
BHOH893
CSER220
CVAL221
CSER222
BLYS86
BLEU192
BPRO193
BHIS196
BILE197
BSER198
BARG218
BPHE219
BALA238
BLEU261
BGLY263
BGLY264
BGLY287
BSER293
BGLN294
BSER389
BGLY390
BGLY391
BGLU392
BLYS421
BTRP422
BLYS451
BTYR452
BMG502
BCA505
BHOH616
BHOH638
BHOH642
BHOH647
BHOH664
BHOH687

site_idAD2
Number of Residues5
Detailsbinding site for residue MG B 502
ChainResidue
BPHE219
BS0N501
BHOH898
BHOH916
BHOH942

site_idAD3
Number of Residues3
Detailsbinding site for residue MG B 503
ChainResidue
BTHR28
BHOH751
BHOH894

site_idAD4
Number of Residues5
Detailsbinding site for residue CA B 505
ChainResidue
BHIS196
BILE197
BTHR289
BS0N501
BHOH861

site_idAD5
Number of Residues3
Detailsbinding site for residue NA B 506
ChainResidue
BGLU4
BTYR140
BHOH992

site_idAD6
Number of Residues32
Detailsbinding site for residue S0N D 501
ChainResidue
DLYS86
DPRO193
DHIS196
DILE197
DSER198
DPHE219
DALA238
DMET242
DLEU261
DGLY263
DGLY264
DGLY287
DSER293
DGLN294
DSER389
DGLY390
DGLY391
DGLU392
DLYS421
DTRP422
DLYS451
DTYR452
DMG502
DHOH620
DHOH641
DHOH671
DHOH707
DHOH709
DHOH763
DHOH834
DHOH850
DHOH855

site_idAD7
Number of Residues5
Detailsbinding site for residue MG D 502
ChainResidue
AHOH720
AHOH787
DPHE219
DS0N501
DHOH868

site_idAD8
Number of Residues3
Detailsbinding site for residue MG D 503
ChainResidue
DLYS320
DGLN359
DTRP362

site_idAD9
Number of Residues1
Detailsbinding site for residue CA D 504
ChainResidue
DHOH948

site_idAE1
Number of Residues2
Detailsbinding site for residue NA D 505
ChainResidue
DGLU355
DPHE358

site_idAE2
Number of Residues4
Detailsbinding site for residue PEG D 506
ChainResidue
BLEU180
BTHR183
DTHR183
DGLU184

site_idAE3
Number of Residues6
Detailsbinding site for residue PEG D 507
ChainResidue
BTHR183
BGLU184
DASN179
DLEU180
DTHR183
DARG258

site_idAE4
Number of Residues5
Detailsbinding site for residue CA C 501
ChainResidue
CTRP188
CSER201
CALA202
CLYS205
CHOH664

site_idAE5
Number of Residues1
Detailsbinding site for residue CA C 502
ChainResidue
BHIS226

site_idAE6
Number of Residues5
Detailsbinding site for residue CA C 503
ChainResidue
CASN179
CPHE283
CTHR297
CLEU298
CSER299

site_idAE7
Number of Residues3
Detailsbinding site for residue CA C 504
ChainResidue
CLYS86
CS0N508
CHOH687

site_idAE8
Number of Residues3
Detailsbinding site for residue NA C 505
ChainResidue
CASN179
CPHE283
CHOH974

site_idAE9
Number of Residues5
Detailsbinding site for residue PEG C 506
ChainResidue
CMET10
CALA13
CGLN14
CPHE35
CHOH945

site_idAF1
Number of Residues3
Detailsbinding site for residue PEG C 507
ChainResidue
CGLY366
CLEU368
CARG382

site_idAF2
Number of Residues38
Detailsbinding site for residue S0N C 508
ChainResidue
CLYS86
CLEU192
CPRO193
CHIS196
CILE197
CSER198
CPHE219
CALA238
CMET242
CLEU261
CGLY263
CGLY264
CGLY287
CSER293
CGLN294
CSER389
CGLY390
CGLY391
CGLU392
CLYS421
CTRP422
CLYS451
CTYR452
CCA504
CMG509
CHOH602
CHOH606
CHOH644
CHOH664
CHOH665
CHOH675
CHOH676
CHOH687
CHOH700
CHOH792
CHOH815
CHOH850
CHOH857

site_idAF3
Number of Residues4
Detailsbinding site for residue MG C 509
ChainResidue
BHOH814
CPHE219
CS0N508
CHOH861

Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. LMYTSGTTGkPK
ChainResidueDetails
ALEU149-LYS160

224931

PDB entries from 2024-09-11

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