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3UPP

Structure of penicillin-binding protein A from M. tuberculosis: ceftrixaone acyl-enzyme complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008360biological_processregulation of cell shape
A0008658molecular_functionpenicillin binding
A0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016787molecular_functionhydrolase activity
A0031504biological_processpeptidoglycan-based cell wall organization
A0071555biological_processcell wall organization
A0071972molecular_functionpeptidoglycan L,D-transpeptidase activity
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008360biological_processregulation of cell shape
B0008658molecular_functionpenicillin binding
B0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016787molecular_functionhydrolase activity
B0031504biological_processpeptidoglycan-based cell wall organization
B0071555biological_processcell wall organization
B0071972molecular_functionpeptidoglycan L,D-transpeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PCZ A 800
ChainResidue
AGLY221
ATHR427
ATHR470
ASER222
ATYR261
ASER281
AASN283
AGLN339
ALYS424
ATHR425
AGLY426

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PCZ B 800
ChainResidue
BSER222
BTYR261
BSER281
BASN283
BTHR425
BGLY426
BTHR427
BGLU429
BSER468
BALA469
BGLY471
BGLY472

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues648
DetailsRegion: {"description":"Transpeptidase"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"UniProtKB","id":"P0AD65","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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