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3WQG

D-threo-3-hydroxyaspartate dehydratase C353A mutant in the metal-free form

Functional Information from GO Data
ChainGOidnamespacecontents
A0008721molecular_functionD-serine ammonia-lyase activity
A0016829molecular_functionlyase activity
A0016841molecular_functionammonia-lyase activity
A0030170molecular_functionpyridoxal phosphate binding
A0036088biological_processD-serine catabolic process
B0008721molecular_functionD-serine ammonia-lyase activity
B0016829molecular_functionlyase activity
B0016841molecular_functionammonia-lyase activity
B0030170molecular_functionpyridoxal phosphate binding
B0036088biological_processD-serine catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PLP A 401
ChainResidue
AHIS41
AALA235
AGLY236
AVAL237
AGOL402
AHOH522
AHOH646
AHOH698
AHOH728
AHOH729
ALYS43
AARG141
AHIS172
ATYR177
AGLY216
ASER217
ATHR218
AARG234

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
ALYS43
AHIS140
AARG141
AHIS172
AGLY174
ATYR177
APLP401
AHOH728
BASN318

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PLP B 401
ChainResidue
BHIS41
BLYS43
BARG141
BHIS172
BTYR177
BGLY216
BSER217
BTHR218
BARG234
BALA235
BGLY236
BVAL237
BGOL402
BHOH517
BHOH618
BHOH673
BHOH701
BHOH702

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 402
ChainResidue
BLYS43
BHIS140
BARG141
BHIS172
BGLY174
BPLP401
BHOH701

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 403
ChainResidue
AASP303
AARG338
AHOH671
AHOH709
BALA154
BARG157
BTHR158
BASP161
BHOH552
BHOH647

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000305
ChainResidueDetails
ALYS43
BLYS43

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PDB entries from 2024-10-16

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