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4D9M

Crystal structure of Diaminopropionate ammonia lyase from Escherichia coli in complex with aminoacrylate-PLP azomethine reaction intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0008838molecular_functiondiaminopropionate ammonia-lyase activity
A0016829molecular_functionlyase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042803molecular_functionprotein homodimerization activity
B0008838molecular_functiondiaminopropionate ammonia-lyase activity
B0016829molecular_functionlyase activity
B0030170molecular_functionpyridoxal phosphate binding
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 0JO A 401
ChainResidue
ALYS77
AALA235
AMET236
AGLY288
ALEU289
ATHR376
AGLU377
AHOH523
ATHR119
AASP120
AASN122
AHIS123
AALA231
AGLY232
AVAL233
AGLY234

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 0JO B 401
ChainResidue
BLYS77
BTHR119
BASP120
BASN122
BHIS123
BGLY232
BVAL233
BGLY234
BALA235
BMET236
BGLY288
BLEU289
BTHR376
BGLU377
BHOH543

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor; for D-DAP ammonia-lyase activity","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor; for L-DAP ammonia-lyase activity","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine"}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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