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6IYV

Crystal sturucture of L,D-transpeptidase LdtMt2 from Mycobacterium tuberculosis in complex with ertapenem adduct

Functional Information from GO Data
ChainGOidnamespacecontents
A0016740molecular_functiontransferase activity
B0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue 2RG B 501
ChainResidue
ALYS299
BGOL506
BHOH622
BHOH624
BHOH693
BHOH742
BHOH757
BHOH774
AGLN363
BMET303
BTYR308
BVAL310
BTYR318
BGLY332
BHIS352
BCYS354

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL B 502
ChainResidue
BASP251
BVAL253
BHIS368
BLYS370
BHOH601
BHOH628
BHOH734
BHOH767
BHOH854

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL B 503
ChainResidue
BGLU213
BHIS214
BPHE215
BILE291
BHOH641
BHOH709
BHOH829

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL B 504
ChainResidue
AGLN400
AGOL503
AHOH639
BASP251
BHOH618

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL B 505
ChainResidue
BTYR366
BASP367
BVAL369
BLYS370

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL B 506
ChainResidue
ATRP324
AGLN363
AASP367
B2RG501
BHOH624
BHOH647

site_idAC7
Number of Residues11
Detailsbinding site for residue PEG B 507
ChainResidue
AARG181
ATRP202
AASN204
AASN405
AHOH702
BGLY161
BVAL222
BHIS246
BPHE247
BTHR248
BHOH609

site_idAC8
Number of Residues8
Detailsbinding site for residue PEG B 508
ChainResidue
ALYS407
BTHR191
BTHR192
BASN193
BASP223
BHOH605
BHOH747
BHOH779

site_idAC9
Number of Residues1
Detailsbinding site for residue SO4 B 509
ChainResidue
BHOH603

site_idAD1
Number of Residues9
Detailsbinding site for residue GOL A 502
ChainResidue
AGLU213
AHIS214
APHE215
AILE291
ATRP394
ATRS507
AHOH711
AHOH728
AHOH819

site_idAD2
Number of Residues7
Detailsbinding site for residue GOL A 503
ChainResidue
ATHR384
ALEU385
AGLY387
AASN395
AILE396
AHOH607
BGOL504

site_idAD3
Number of Residues6
Detailsbinding site for residue GOL A 504
ChainResidue
AGLN327
AHOH657
AHOH660
BHIS150
BLEU151
BHOH626

site_idAD4
Number of Residues7
Detailsbinding site for residue GOL A 505
ChainResidue
AARG173
AASN204
AARG206
AHOH612
AHOH733
AHOH793
BHIS150

site_idAD5
Number of Residues6
Detailsbinding site for residue GOL A 506
ChainResidue
ALYS370
AASP373
AHOH713
AASP251
AVAL253
AHIS368

site_idAD6
Number of Residues2
Detailsbinding site for residue TRS A 507
ChainResidue
AGLU376
AGOL502

site_idAD7
Number of Residues20
Detailsbinding site for Di-peptide 2RG A 501 and CYS A 354
ChainResidue
ASER279
AMET280
AMET303
ATHR307
ATYR308
ATYR318
AGLY332
AVAL333
APHE334
AHIS336
ASER351
AHIS352
AGLY353
ALEU355
AASN356
AHOH628
AHOH677
AHOH796
BPRO148
BHOH727

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01373, ECO:0000305|PubMed:23519417
ChainResidueDetails
BHIS336
AHIS336

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01373, ECO:0000269|PubMed:23519417
ChainResidueDetails
BCYS354
ACYS354

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
BASP232
BGLU235
BGLY236
AASP232
AGLU235
AGLY236

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BTYR318
BSER331
BASN356
ATYR318
ASER331
AASN356

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Binds to carbapenem drug (covalent)
ChainResidueDetails
BCYS354
ACYS354

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PDB entries from 2024-08-07

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