Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6X9F

Pseudomonas aeruginosa MurC with AZ8074

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008360biological_processregulation of cell shape
A0008763molecular_functionUDP-N-acetylmuramate-L-alanine 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
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0008360biological_processregulation of cell shape
B0008763molecular_functionUDP-N-acetylmuramate-L-alanine 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
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0008360biological_processregulation of cell shape
C0008763molecular_functionUDP-N-acetylmuramate-L-alanine ligase activity
C0009058biological_processbiosynthetic process
C0009252biological_processpeptidoglycan biosynthetic process
C0016874molecular_functionligase activity
C0016881molecular_functionacid-amino acid ligase activity
C0051301biological_processcell division
C0071555biological_processcell wall organization
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0008360biological_processregulation of cell shape
D0008763molecular_functionUDP-N-acetylmuramate-L-alanine ligase activity
D0009058biological_processbiosynthetic process
D0009252biological_processpeptidoglycan biosynthetic process
D0016874molecular_functionligase activity
D0016881molecular_functionacid-amino acid ligase activity
D0051301biological_processcell division
D0071555biological_processcell wall organization
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0008360biological_processregulation of cell shape
E0008763molecular_functionUDP-N-acetylmuramate-L-alanine ligase activity
E0009058biological_processbiosynthetic process
E0009252biological_processpeptidoglycan biosynthetic process
E0016874molecular_functionligase activity
E0016881molecular_functionacid-amino acid ligase activity
E0051301biological_processcell division
E0071555biological_processcell wall organization
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0008360biological_processregulation of cell shape
F0008763molecular_functionUDP-N-acetylmuramate-L-alanine ligase activity
F0009058biological_processbiosynthetic process
F0009252biological_processpeptidoglycan biosynthetic process
F0016874molecular_functionligase activity
F0016881molecular_functionacid-amino acid ligase activity
F0051301biological_processcell division
F0071555biological_processcell wall organization
G0005524molecular_functionATP binding
G0005737cellular_componentcytoplasm
G0008360biological_processregulation of cell shape
G0008763molecular_functionUDP-N-acetylmuramate-L-alanine ligase activity
G0009058biological_processbiosynthetic process
G0009252biological_processpeptidoglycan biosynthetic process
G0016874molecular_functionligase activity
G0016881molecular_functionacid-amino acid ligase activity
G0051301biological_processcell division
G0071555biological_processcell wall organization
H0005524molecular_functionATP binding
H0005737cellular_componentcytoplasm
H0008360biological_processregulation of cell shape
H0008763molecular_functionUDP-N-acetylmuramate-L-alanine ligase activity
H0009058biological_processbiosynthetic process
H0009252biological_processpeptidoglycan biosynthetic process
H0016874molecular_functionligase activity
H0016881molecular_functionacid-amino acid ligase activity
H0051301biological_processcell division
H0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue UXP A 501
ChainResidue
AHIS117
CEDO502
AGLY118
ATHR182
AASN183
ACYS219
ATYR239
AHIS281
ALEU284
AASN285

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 502
ChainResidue
APRO266
AVAL291
AASP295
AHOH602

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 503
ChainResidue
APRO96
AGLU99
AHIS173
GHIS208
GARG234

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 504
ChainResidue
AASP221
ALEU280
ALEU284
CASP222
CPRO223

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 505
ChainResidue
APRO270
ALEU271
AASP272

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 506
ChainResidue
AALA19
AGLY20
ACYS22
AGLY23
ALEU145

site_idAC7
Number of Residues6
Detailsbinding site for residue DMS A 507
ChainResidue
ALEU135
AARG158
ATYR159
AGLU296
AGLY297
AILE298

site_idAC8
Number of Residues9
Detailsbinding site for residue UXP B 501
ChainResidue
BGLY118
BTHR182
BASN183
BCYS219
BTYR239
BHIS281
BLEU284
BASN285
HHOH603

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO B 502
ChainResidue
BARG108
BALA156
BARG158
BHOH622
DHOH629

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO B 503
ChainResidue
BPRO96
BGLU99
EHIS208
EARG234

site_idAD2
Number of Residues4
Detailsbinding site for residue EDO B 504
ChainResidue
BHIS109
BARG158
BTYR159
BGLU296

site_idAD3
Number of Residues6
Detailsbinding site for residue EDO B 505
ChainResidue
BASP221
BLEU280
BLEU284
HILE184
HASP222
HPRO223

site_idAD4
Number of Residues4
Detailsbinding site for residue EDO B 506
ChainResidue
BPRO270
BLEU271
BASP272
BHOH625

site_idAD5
Number of Residues5
Detailsbinding site for residue EDO B 507
ChainResidue
BALA19
BGLY23
BARG144
BLEU145
BHOH644

site_idAD6
Number of Residues4
Detailsbinding site for residue DMS B 508
ChainResidue
BARG226
BTHR238
BASP244
EARG91

site_idAD7
Number of Residues6
Detailsbinding site for residue DMS B 509
ChainResidue
BLEU135
BARG158
BGLU296
BGLY297
BHOH613
DHOH645

site_idAD8
Number of Residues2
Detailsbinding site for residue DMS B 510
ChainResidue
BPRO93
BVAL94

site_idAD9
Number of Residues9
Detailsbinding site for residue DMS B 511
ChainResidue
BVAL220
BASP221
BPRO223
BARG226
HVAL220
HASP221
HPRO223
HARG226
HHOH636

site_idAE1
Number of Residues3
Detailsbinding site for residue DMS B 512
ChainResidue
BARG9
BLEU31
BTYR33

site_idAE2
Number of Residues10
Detailsbinding site for residue UXP C 501
ChainResidue
CHIS117
CGLY118
CTHR182
CASN183
CCYS219
CTYR239
CHIS281
CLEU284
CASN285
CEDO502

site_idAE3
Number of Residues6
Detailsbinding site for residue EDO C 502
ChainResidue
APRO223
AUXP501
CASP221
CLEU280
CLEU284
CUXP501

site_idAE4
Number of Residues7
Detailsbinding site for residue EDO C 503
ChainResidue
AVAL220
AASP221
AARG226
AHOH654
CVAL220
CASP221
CPRO223

site_idAE5
Number of Residues4
Detailsbinding site for residue EDO C 504
ChainResidue
CTHR238
CASP244
CALA245
DARG91

site_idAE6
Number of Residues5
Detailsbinding site for residue EDO C 505
ChainResidue
AASN251
CPHE196
CASN197
CLYS200
CGLU227

site_idAE7
Number of Residues7
Detailsbinding site for residue EDO C 506
ChainResidue
APHE196
AASN197
ALYS200
AGLU227
CASN251
CILE252
CHOH658

site_idAE8
Number of Residues9
Detailsbinding site for residue UXP D 501
ChainResidue
DHIS117
DGLY118
DTHR182
DASN183
DCYS219
DTYR239
DHIS281
DLEU284
DASN285

site_idAE9
Number of Residues6
Detailsbinding site for residue EDO D 502
ChainResidue
CHIS208
CARG234
DPRO96
DGLU99
DHIS173
DHOH643

site_idAF1
Number of Residues3
Detailsbinding site for residue EDO D 503
ChainResidue
DPRO270
DASP272
DHOH631

site_idAF2
Number of Residues4
Detailsbinding site for residue EDO D 504
ChainResidue
DPRO266
DASP295
DHOH615
DHOH616

site_idAF3
Number of Residues4
Detailsbinding site for residue EDO D 505
ChainResidue
DSER124
DALA127
DPHE139
DPHE310

site_idAF4
Number of Residues6
Detailsbinding site for residue DMS D 506
ChainResidue
DARG158
DTYR159
DGLU296
DGLY297
DILE298
DHOH603

site_idAF5
Number of Residues8
Detailsbinding site for residue DMS D 507
ChainResidue
DVAL220
DASP221
DASP222
DPRO223
DARG226
GVAL220
GASP221
GPRO223

site_idAF6
Number of Residues1
Detailsbinding site for residue CL D 508
ChainResidue
DVAL94

site_idAF7
Number of Residues8
Detailsbinding site for residue UXP E 501
ChainResidue
EGLY118
ETHR182
EASN183
ECYS219
ETYR239
EHIS281
ELEU284
EASN285

site_idAF8
Number of Residues2
Detailsbinding site for residue EDO E 502
ChainResidue
EHOH633
FASP244

site_idAF9
Number of Residues5
Detailsbinding site for residue EDO E 503
ChainResidue
EASN197
ELYS200
EGLU227
EHOH604
FALA249

site_idAG1
Number of Residues3
Detailsbinding site for residue EDO E 504
ChainResidue
EPRO270
EASP272
EHOH602

site_idAG2
Number of Residues6
Detailsbinding site for residue EDO E 505
ChainResidue
BLEU172
BHIS173
BASN209
ELEU172
EGLU205
EASN209

site_idAG3
Number of Residues2
Detailsbinding site for residue DMS E 506
ChainResidue
ETYR159
EGLU296

site_idAG4
Number of Residues4
Detailsbinding site for residue DMS E 507
ChainResidue
EARG9
ELEU31
EGLY32
ETYR33

site_idAG5
Number of Residues1
Detailsbinding site for residue CL E 508
ChainResidue
EVAL94

site_idAG6
Number of Residues9
Detailsbinding site for residue UXP F 501
ChainResidue
FHIS117
FGLY118
FTHR182
FASN183
FCYS219
FTYR239
FHIS281
FLEU284
FASN285

site_idAG7
Number of Residues4
Detailsbinding site for residue EDO F 502
ChainResidue
FLEU229
FTHR238
FASP244
FALA245

site_idAG8
Number of Residues5
Detailsbinding site for residue EDO F 503
ChainResidue
FPRO96
FGLU99
FHIS173
HHIS208
HARG234

site_idAG9
Number of Residues3
Detailsbinding site for residue EDO F 504
ChainResidue
FPRO270
FLEU271
FASP272

site_idAH1
Number of Residues5
Detailsbinding site for residue DMS F 505
ChainResidue
FARG158
FTYR159
FGLU296
FHOH620
FHOH638

site_idAH2
Number of Residues1
Detailsbinding site for residue CL F 506
ChainResidue
FVAL94

site_idAH3
Number of Residues10
Detailsbinding site for residue UXP G 501
ChainResidue
GHIS117
GGLY118
GTHR182
GASN183
GCYS219
GTYR239
GHIS281
GLEU284
GASN285
GHOH629

site_idAH4
Number of Residues5
Detailsbinding site for residue EDO G 502
ChainResidue
AHIS208
AARG234
GPRO96
GGLU99
GHIS173

site_idAH5
Number of Residues3
Detailsbinding site for residue EDO G 503
ChainResidue
GPRO270
GLEU271
GASP272

site_idAH6
Number of Residues4
Detailsbinding site for residue DMS G 504
ChainResidue
FHOH604
GTYR159
GGLU296
GGLY297

site_idAH7
Number of Residues1
Detailsbinding site for residue CL G 505
ChainResidue
GVAL94

site_idAH8
Number of Residues9
Detailsbinding site for residue UXP H 501
ChainResidue
HHIS117
HGLY118
HTHR182
HASN183
HCYS219
HTYR239
HHIS281
HLEU284
HASN285

site_idAH9
Number of Residues5
Detailsbinding site for residue EDO H 502
ChainResidue
FHIS208
FARG234
HPRO96
HGLU99
HHIS173

site_idAI1
Number of Residues5
Detailsbinding site for residue EDO H 503
ChainResidue
BPRO223
HASP221
HLEU241
HLEU284
HHOH603

site_idAI2
Number of Residues3
Detailsbinding site for residue EDO H 504
ChainResidue
HPRO270
HASP272
HHOH630

site_idAI3
Number of Residues4
Detailsbinding site for residue DMS H 505
ChainResidue
HARG158
HTYR159
HGLU296
HHOH612

site_idAI4
Number of Residues1
Detailsbinding site for residue CL H 506
ChainResidue
HVAL94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00046
ChainResidueDetails
AGLY115
BGLY115
CGLY115
DGLY115
EGLY115
FGLY115
GGLY115
HGLY115

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon