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5GJO

Crystal structure of SrLDC mutant (A225C/T302C) in complex with PLP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004586molecular_functionornithine decarboxylase activity
A0005737cellular_componentcytoplasm
A0006596biological_processpolyamine biosynthetic process
A0008295biological_processspermidine biosynthetic process
A0008923molecular_functionlysine decarboxylase activity
A0009446biological_processputrescine biosynthetic process
A0016831molecular_functioncarboxy-lyase activity
A0033387biological_processputrescine biosynthetic process from ornithine
B0003824molecular_functioncatalytic activity
B0004586molecular_functionornithine decarboxylase activity
B0005737cellular_componentcytoplasm
B0006596biological_processpolyamine biosynthetic process
B0008295biological_processspermidine biosynthetic process
B0008923molecular_functionlysine decarboxylase activity
B0009446biological_processputrescine biosynthetic process
B0016831molecular_functioncarboxy-lyase activity
B0033387biological_processputrescine biosynthetic process from ornithine
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 401
ChainResidue
ALYS143
ASER186
ATHR187
AALA188
AHOH613
BARG245

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 402
ChainResidue
BLYS275
BARG277
ATHR150
AGLY153
AHOH639

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 403
ChainResidue
AARG5
AHIS306
AHOH602
AHOH658

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 404
ChainResidue
ASER7
AGLU8
AHOH512
AHOH641
AHOH744

site_idAC5
Number of Residues9
Detailsbinding site for residue GOL A 405
ChainResidue
ATHR358
AARG359
APHE360
AHOH569
AHOH652
AHOH764
BSER354
BVAL355
BALA357

site_idAC6
Number of Residues15
Detailsbinding site for residue PLP A 406
ChainResidue
AALA49
ALYS51
AASP70
AHIS179
ASER182
AGLY218
AGLY219
AGLU255
AGLY257
AARG258
ATYR352
AHOH516
AHOH520
AHOH556
BCYS323

site_idAC7
Number of Residues4
Detailsbinding site for residue NA A 407
ChainResidue
AGLU157
AARG199
AHOH515
BARG199

site_idAC8
Number of Residues5
Detailsbinding site for residue NA A 408
ChainResidue
ATYR298
BSER294
BSER356
BTHR358
BNA405

site_idAC9
Number of Residues5
Detailsbinding site for residue NA A 409
ChainResidue
AARG199
AASP202
BARG140
BGLU192
BHOH733

site_idAD1
Number of Residues5
Detailsbinding site for residue SO4 B 401
ChainResidue
AARG245
BLYS143
BSER186
BTHR187
BALA188

site_idAD2
Number of Residues3
Detailsbinding site for residue SO4 B 402
ChainResidue
BSER7
BGLU8
BHOH528

site_idAD3
Number of Residues9
Detailsbinding site for residue GOL B 403
ChainResidue
ASER354
AVAL355
AALA357
AHOH569
BTHR358
BARG359
BPHE360
BHOH576
BHOH688

site_idAD4
Number of Residues16
Detailsbinding site for residue PLP B 404
ChainResidue
ACYS323
BALA49
BLYS51
BASP70
BALA93
BHIS179
BSER182
BGLY218
BGLY219
BGLU255
BGLY257
BARG258
BTYR352
BHOH515
BHOH565
BHOH619

site_idAD5
Number of Residues5
Detailsbinding site for residue NA B 405
ChainResidue
ASER294
ASER356
ATHR358
ANA408
BTYR298

Functional Information from PROSITE/UniProt
site_idPS00878
Number of Residues19
DetailsODR_DC_2_1 Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site. YAmKANptpeILslLaglG
ChainResidueDetails
ATYR48-GLY66

site_idPS00879
Number of Residues18
DetailsODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. AeemgmhLtDLDIGGGFP
ChainResidueDetails
AALA204-PRO221

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor; shared with dimeric partner => ECO:0000250
ChainResidueDetails
ACYS323
BCYS323

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS51
BLYS51

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PDB entries from 2024-11-06

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