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5BWA

Crystal structure of ODC-PLP-AZ1 ternary complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001822biological_processkidney development
A0003824molecular_functioncatalytic activity
A0004586molecular_functionornithine decarboxylase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006595biological_processpolyamine metabolic process
A0006596biological_processpolyamine biosynthetic process
A0008283biological_processcell population proliferation
A0008284biological_processpositive regulation of cell population proliferation
A0009615biological_processresponse to virus
A0016829molecular_functionlyase activity
A0016831molecular_functioncarboxy-lyase activity
A0033387biological_processputrescine biosynthetic process from arginine, via ornithine
A0042176biological_processregulation of protein catabolic process
A0042803molecular_functionprotein homodimerization activity
B0008073molecular_functionornithine decarboxylase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue PLP A 600
ChainResidue
ALYS69
AASP88
AALA111
AHIS197
AGLY237
AGLU274
AGLY276
AARG277
ATYR389

Functional Information from PROSITE/UniProt
site_idPS00878
Number of Residues19
DetailsODR_DC_2_1 Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site. YAvKCNdskaIVktLaatG
ChainResidueDetails
ATYR66-GLY84

site_idPS00879
Number of Residues18
DetailsODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. GaevgfsMyLLDIGGGFP
ChainResidueDetails
AGLY222-PRO239

site_idPS01337
Number of Residues9
DetailsODC_AZ Ornithine decarboxylase antizyme signature. LLEFAEEQL
ChainResidueDetails
BLEU159-LEU167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor; shared with dimeric partner","evidences":[{"source":"PubMed","id":"10623504","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17407445","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OO0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17407445","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26305948","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26443277","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OO0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P07805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P07805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates","evidences":[{"source":"UniProtKB","id":"P00860","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"26305948","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17407445","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"S-nitrosocysteine; in inhibited form","evidences":[{"source":"PubMed","id":"11461922","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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