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4QTF

Structure and specificity of L-D-Transpeptidase from Mycobacterium tuberculosis and antibiotic resistance: Calcium binding promotes dimer formation

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008360biological_processregulation of cell shape
A0009252biological_processpeptidoglycan biosynthetic process
A0016020cellular_componentmembrane
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
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MLD A 501
ChainResidue
ALEU62
ATHR63
AALA64
ASER65
ATHR67
ASER80
AARG139

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 3V5 A 502
ChainResidue
AGLY332
APHE334
AHIS336
AHIS352
AGLY353
ACYS354
AMET303
ASER331

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01373, ECO:0000305|PubMed:23519417
ChainResidueDetails
AHIS336

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01373, ECO:0000269|PubMed:23519417
ChainResidueDetails
ACYS354

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AASP232
AGLU235
AGLY236

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATYR318
ASER331
AASN356

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Binds to carbapenem drug (covalent)
ChainResidueDetails
ACYS354

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PDB entries from 2025-07-02

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