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7B61

Crystal structure of MurE from E.coli in complex with Z57299526

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008360biological_processregulation of cell shape
A0008765molecular_functionUDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity
A0009058biological_processbiosynthetic process
A0009252biological_processpeptidoglycan biosynthetic process
A0016874molecular_functionligase activity
A0016881molecular_functionacid-amino acid ligase activity
A0051301biological_processcell division
A0071555biological_processcell wall organization
B0000287molecular_functionmagnesium ion binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008360biological_processregulation of cell shape
B0008765molecular_functionUDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity
B0009058biological_processbiosynthetic process
B0009252biological_processpeptidoglycan biosynthetic process
B0016874molecular_functionligase activity
B0016881molecular_functionacid-amino acid ligase activity
B0051301biological_processcell division
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue CIT A 501
ChainResidue
ATHR117
AASN118
AGLY119
ALYS120
ATHR121
ATHR143
AHOH622
AHOH692

site_idAC2
Number of Residues12
Detailsbinding site for residue SYQ A 502
ChainResidue
ALEU250
ALEU253
APRO254
AALA256
AALA258
AHIS264
AILE265
AASN266
ACYS269
AGLY271
AARG272
AARG247

site_idAC3
Number of Residues9
Detailsbinding site for residue T3Z A 503
ChainResidue
ATHR115
ALEU189
APHE199
ASER202
ATYR229
ACYS234
AILE239
ATRP249
AHOH696

site_idAC4
Number of Residues5
Detailsbinding site for residue IPA A 504
ChainResidue
AARG110
ALEU322
AGLY323
ATYR324
BASP107

site_idAC5
Number of Residues4
Detailsbinding site for residue IPA A 505
ChainResidue
AARG247
AHIS264
AHOH686
BARG335

site_idAC6
Number of Residues9
Detailsbinding site for residue T3Z B 501
ChainResidue
BTHR115
BLEU189
BPHE199
BSER202
BTYR229
BCYS234
BILE239
BTRP249
BHOH705

site_idAC7
Number of Residues7
Detailsbinding site for residue CIT B 502
ChainResidue
BTHR117
BASN118
BGLY119
BLYS120
BTHR121
BTHR143
BHOH650

site_idAC8
Number of Residues4
Detailsbinding site for residue DMS B 503
ChainResidue
BGLU222
BTRP226
BVAL245
BTRP249

site_idAC9
Number of Residues11
Detailsbinding site for residue SYQ B 504
ChainResidue
BARG247
BALA251
BLEU253
BPRO254
BALA256
BALA258
BHIS264
BILE265
BASN266
BGLY271
BARG272

site_idAD1
Number of Residues5
Detailsbinding site for residue IPA B 505
ChainResidue
BARG110
BGLU136
BLEU322
BGLY323
BTYR324

site_idAD2
Number of Residues3
Detailsbinding site for residue IPA B 506
ChainResidue
BMET261
BALA276
BTHR277

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING:
ChainResidueDetails
ALEU27
AASP414
AGLY465
AGLU469
BLEU27
BSER29
BHIS44
BASN157
BTHR158
BSER185
BGLN191
ASER29
BARG193
BARG390
BASP414
BGLY465
BGLU469
AHIS44
AASN157
ATHR158
ASER185
AGLN191
AARG193
AARG390

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY116
BGLY116

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000269|PubMed:11124264
ChainResidueDetails
ALYS225
BLYS225

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PDB entries from 2024-07-24

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