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5BUS

O-succinylbenzoate Coenzyme A Synthetase (MenE) from Bacillus Subtilis, in complex with AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0008756molecular_functiono-succinylbenzoate-CoA ligase activity
A0009234biological_processmenaquinone biosynthetic process
A0016405molecular_functionCoA-ligase activity
A0016878molecular_functionacid-thiol ligase activity
B0005524molecular_functionATP binding
B0008756molecular_functiono-succinylbenzoate-CoA ligase activity
B0009234biological_processmenaquinone biosynthetic process
B0016405molecular_functionCoA-ligase activity
B0016878molecular_functionacid-thiol ligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue CL A 501
ChainResidue
BLEU178

site_idAC2
Number of Residues11
Detailsbinding site for residue AMP A 503
ChainResidue
AVAL379
AARG382
ALYS471
AHIS196
AGLY264
AGLY265
ASER285
AGLY287
AMET288
ATHR289
AASP367

site_idAC3
Number of Residues1
Detailsbinding site for residue CL B 501
ChainResidue
BASP107

site_idAC4
Number of Residues2
Detailsbinding site for residue CL B 502
ChainResidue
BARG187
BHIS231

site_idAC5
Number of Residues7
Detailsbinding site for residue AMP B 503
ChainResidue
BHIS196
BGLY264
BSER285
BGLY287
BMET288
BTHR289
BASP367

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsRegion: {"description":"Required for acetyltransferase recognition","evidences":[{"source":"PubMed","id":"39422507","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsMotif: {"description":"LLG motif","evidences":[{"source":"PubMed","id":"26276389","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27933791","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28559280","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00731","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26276389","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BUR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26276389","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27933791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BUS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5GTD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28559280","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5X8F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5X8G","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27933791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5GTD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PDB","id":"5X8F","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Hinge for 140 degree angle conformational rotation during catalysis","evidences":[{"source":"PubMed","id":"28559280","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by AcuA","evidences":[{"source":"PubMed","id":"39422507","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

256158

PDB entries from 2026-07-08

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