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1Z6F

Crystal structure of penicillin-binding protein 5 from E. coli in complex with a boronic acid inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000270biological_processpeptidoglycan metabolic process
A0004180molecular_functioncarboxypeptidase activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008360biological_processregulation of cell shape
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042803molecular_functionprotein homodimerization activity
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE BO9 A 401
ChainResidue
AALA43
AHOH683
AHOH847
ASER44
ALYS47
AGLY85
ASER86
ASER87
AASN112
AGLY215
AHIS216

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AASN134
AVAL137
AASN138
ATHR145
AHIS146
AGLN343
AHOH775
AHOH819

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASER44

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ALYS47

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
ASER110

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS213

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
ASER44
ALYS47
AGLN148
ASER110

219140

PDB entries from 2024-05-01

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