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5GJP

Crystal structure of SrLDC in complex with PLP and Cadaverine

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
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue N2P A 401
ChainResidue
ASER182
AARG258
ATYR290
ATYR298
AASP299
AASP324
ATYR352
APLP402

site_idAC2
Number of Residues13
Detailsbinding site for residue PLP A 402
ChainResidue
AASP70
AHIS179
ASER182
AGLY218
AGLY219
AGLU255
AGLY257
AARG258
ACYS323
ATYR352
AN2P401
AHOH508
ALYS51

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 403
ChainResidue
AALA99
ALYS123
AILE272

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 404
ChainResidue
ALYS2
ASER26
AGLU32
APGE405

site_idAC5
Number of Residues10
Detailsbinding site for residue PGE A 405
ChainResidue
AMET1
ALYS29
AGLU32
AASN33
APHE36
APRO223
ALEU232
ATYR259
ATHR263
AGOL404

site_idAC6
Number of Residues1
Detailsbinding site for residue NA A 406
ChainResidue
AGLU348

site_idAC7
Number of Residues2
Detailsbinding site for residue MG A 408
ChainResidue
AALA357
AARG359

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 Residues1
DetailsACT_SITE: Proton donor; shared with dimeric partner => ECO:0000250
ChainResidueDetails
ACYS323

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS51

222036

PDB entries from 2024-07-03

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