3PTE

THE REFINED CRYSTALLOGRAPHIC STRUCTURE OF A DD-PEPTIDASE PENICILLIN-TARGET ENZYME AT 1.6 A RESOLUTION

Replaces:  1PTE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004180	molecular_function	carboxypeptidase activity
A	0005576	cellular_component	extracellular region
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008360	biological_process	regulation of cell shape
A	0009002	molecular_function	serine-type D-Ala-D-Ala carboxypeptidase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016787	molecular_function	hydrolase activity
A	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	ACT
Number of Residues	8
Details

Chain	Residue
A	SER62
A	LYS65
A	TYR159
A	SER160
A	ASN161
A	HIS298
A	THR299
A	GLY300

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PubMed","id":"12215418","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12564922","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15581896","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12215418","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12564922","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15581896","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1ei5

Chain	Residue	Details
A	HIS298
A	SER62
A	ASN161
A	LYS65
A	TYR159

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