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2EX9

Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with penicillin-V

Functional Information from GO Data
ChainGOidnamespacecontents
A0000270biological_processpeptidoglycan metabolic process
A0004175molecular_functionendopeptidase activity
A0004180molecular_functioncarboxypeptidase activity
A0004185molecular_functionserine-type carboxypeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008360biological_processregulation of cell shape
A0008658molecular_functionpenicillin binding
A0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016787molecular_functionhydrolase activity
A0042597cellular_componentperiplasmic space
A0043093biological_processFtsZ-dependent cytokinesis
A0046677biological_processresponse to antibiotic
A0051301biological_processcell division
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 35P A 501
ChainResidue
ASER62
AHOH1188
APHE160
ASER306
AASN308
ASER420
ALEU421
AGLN422
AHOH1130
AHOH1143

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 601
ChainResidue
AARG117
AGLY412
ALYS413
ASER415
APHE430
AILE431
ATHR432
AARG438
AHOH1241

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000250|UniProtKB:P39844
ChainResidueDetails
ASER62

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P39844
ChainResidueDetails
ALYS65

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P39844
ChainResidueDetails
ASER306

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS417

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PDB entries from 2024-11-06

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