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4JMX

Structure of LD transpeptidase LdtMt1 in complex with imipenem

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008360biological_processregulation of cell shape
A0009252biological_processpeptidoglycan biosynthetic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0018104biological_processpeptidoglycan-protein cross-linking
A0042597cellular_componentperiplasmic space
A0071555biological_processcell wall organization
A0071972molecular_functionpeptidoglycan L,D-transpeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE IM2 A 301
ChainResidue
AMET175
AASN228
AHOH474
ATYR190
AGLY204
AHIS208
ATRP212
ASER223
AHIS224
AGLY225
ACYS226

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:23999293
ChainResidueDetails
AHIS208

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01373, ECO:0000269|PubMed:23999293
ChainResidueDetails
ACYS226

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATYR190
ASER203
AASN228

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.2, ECO:0007744|PDB:4JMX
ChainResidueDetails
AHIS208
AHIS224

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: covalent => ECO:0000269|Ref.2, ECO:0007744|PDB:4JMX
ChainResidueDetails
ACYS226

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PDB entries from 2024-07-10

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