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4D9G

Crystal structure of Selenomethionine incorporated holo Diaminopropionate ammonia lyase from Escherichia coli

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 Residues10
DetailsBINDING SITE FOR RESIDUE TRS A 401
ChainResidue
ALLP77
AHOH574
AASP120
ATYR168
AASP189
AVAL233
AGLY288
ALEU289
AALA290
AHOH573

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS B 401
ChainResidue
BLLP77
BASP120
BASP189
BVAL233
BGLY288
BLEU289
BALA290
BHOH504
BHOH537

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor; for D-DAP ammonia-lyase activity => ECO:0000305
ChainResidueDetails
ALLP77
BLLP77

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor; for L-DAP ammonia-lyase activity => ECO:0000305
ChainResidueDetails
AASP120
BASP120

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALLP77
BLLP77

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PDB entries from 2024-11-06

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