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5D7H

X-RAY CRYSTAL STRUCTURE OF L,D TRANSPEPTIDASE 2 FROM MYCOBACTERIUM TUBERCULOSIS

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008360biological_processregulation of cell shape
A0009252biological_processpeptidoglycan biosynthetic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0018104biological_processpeptidoglycan-protein cross-linking
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
A0071972molecular_functionpeptidoglycan L,D-transpeptidase activity
B0005886cellular_componentplasma membrane
B0008360biological_processregulation of cell shape
B0009252biological_processpeptidoglycan biosynthetic process
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0018104biological_processpeptidoglycan-protein cross-linking
B0046872molecular_functionmetal ion binding
B0071555biological_processcell wall organization
B0071972molecular_functionpeptidoglycan L,D-transpeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 A 501
ChainResidue
AARG104
APRO107
ASO4505
AHOH619

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 502
ChainResidue
AGLY234
AGLU235
AHOH610

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 503
ChainResidue
AARG122
BPRO311
BVAL312
BASN313
AARG99
AGLU116

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 504
ChainResidue
AARG297
AARG371
AHOH604

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 505
ChainResidue
ASER106
AARG111
ASO4501

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 506
ChainResidue
AHIS336
ATRP340
ASER351
AHIS352
ACYS354
AASN356

site_idAC7
Number of Residues4
Detailsbinding site for residue GOL A 507
ChainResidue
AASN177
AASN204
AASN205
AHOH605

site_idAC8
Number of Residues2
Detailsbinding site for residue GOL A 508
ChainResidue
AGLU176
AARG206

site_idAC9
Number of Residues2
Detailsbinding site for residue SO4 A 509
ChainResidue
AHIS300
BHIS150

site_idAD1
Number of Residues5
Detailsbinding site for residue SO4 B 501
ChainResidue
BARG297
BARG371
BHOH604
BHOH628
BHOH690

site_idAD2
Number of Residues5
Detailsbinding site for residue SO4 B 502
ChainResidue
BASN177
BASN205
BARG206
BHOH613
BHOH681

site_idAD3
Number of Residues7
Detailsbinding site for residue SO4 B 503
ChainResidue
BHIS336
BTRP340
BSER351
BHIS352
BCYS354
BASN356
BHOH608

site_idAD4
Number of Residues3
Detailsbinding site for residue SO4 B 504
ChainResidue
BARG104
BSER106
BARG111

site_idAD5
Number of Residues5
Detailsbinding site for residue SO4 B 505
ChainResidue
BARG123
BTHR142
BSER358
BPRO359
BSER360

site_idAD6
Number of Residues3
Detailsbinding site for residue SO4 B 506
ChainResidue
BASN205
BHOH611
BHOH681

site_idAD7
Number of Residues1
Detailsbinding site for residue SO4 B 507
ChainResidue
BLYS189

site_idAD8
Number of Residues2
Detailsbinding site for residue GOL B 508
ChainResidue
BGLU176
BARG206

site_idAD9
Number of Residues2
Detailsbinding site for residue GOL B 509
ChainResidue
BGLU271
BVAL272

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
AHIS336
BHIS336

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

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

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

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

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PDB entries from 2024-11-06

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