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4DZA

Crystal structure of a lysine racemase within internal aldimine linkage

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006522biological_processalanine metabolic process
A0008784molecular_functionalanine racemase activity
A0016853molecular_functionisomerase activity
Functional Information from PROSITE/UniProt
site_idPS00395
Number of Residues11
DetailsALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVlKGDAYGHD
ChainResidueDetails
AALA71-ASP81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000305|PubMed:23118975
ChainResidueDetails
ALLP74
ATYR299

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02212
ChainResidueDetails
AMET347
AARG173

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:23118975, ECO:0000269|DOI:10.1016/j.procbio.2011.06.019
ChainResidueDetails
ALLP74

site_idSWS_FT_FI4
Number of Residues1
DetailsLIPID: S-diacylglycerol cysteine => ECO:0000255|PROSITE-ProRule:PRU00303
ChainResidueDetails
ACYS19

221051

PDB entries from 2024-06-12

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