4DZA

Crystal structure of a lysine racemase within internal aldimine linkage

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0006522	biological_process	alanine metabolic process
A	0008784	molecular_function	alanine racemase activity
A	0016853	molecular_function	isomerase activity

Functional Information from PROSITE/UniProt

site_id	PS00395
Number of Residues	11
Details	ALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVlKGDAYGHD

Chain	Residue	Details
A	ALA71-ASP81

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_02212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23118975","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02212","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_02212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23118975","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2011","firstPage":"1914","lastPage":"1920","volume":"46","journal":"Process Biochem.","title":"Biochemical characterization of a novel lysine racemase from Proteus mirabilis BCRC10725.","authors":["Kuana Y.C.","Kaob C.H.","Chenc C.H.","Chend C.C.","Hue H.Y.","Hsua W.H."],"citationCrossReferences":[{"database":"DOI","id":"10.1016/j.procbio.2011.06.019"}]}}]}

Chain

Residue

Details

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