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4PB4

D-threo-3-hydroxyaspartate dehydratase H351A mutant complexed with 2-amino maleic acid

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 Residues6
Detailsbinding site for residue MG A 402
ChainResidue
ACYS353
A2KZ403
AHOH674
AHOH675
AHOH676
AHOH709

site_idAC2
Number of Residues6
Detailsbinding site for residue MG B 402
ChainResidue
BHOH670
BHOH671
BHOH712
BCYS353
B2KZ403
BHOH669

site_idAC3
Number of Residues23
Detailsbinding site for residues PLP A 401 and 2KZ A 403
ChainResidue
AHIS41
ALYS43
AARG141
AHIS172
ATYR177
ASER217
ATHR218
AARG234
AALA235
AGLY236
AVAL237
AMG402
AHOH549
AHOH615
AHOH619
AHOH639
AHOH674
AHOH675
AHOH676
AHOH709
AHOH710
BASN318
BGLN319

site_idAC4
Number of Residues23
Detailsbinding site for residues PLP B 401 and 2KZ B 403
ChainResidue
AASN318
AGLN319
BHIS41
BLYS43
BARG141
BHIS172
BTYR177
BSER217
BTHR218
BARG234
BALA235
BGLY236
BVAL237
BMG402
BHOH551
BHOH573
BHOH604
BHOH619
BHOH669
BHOH670
BHOH671
BHOH712
BHOH713

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 2024-07-10

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