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7ODC

CRYSTAL STRUCTURE ORNITHINE DECARBOXYLASE FROM MOUSE, TRUNCATED 37 RESIDUES FROM THE C-TERMINUS, TO 1.6 ANGSTROM RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0001822biological_processkidney development
A0003824molecular_functioncatalytic activity
A0004586molecular_functionornithine decarboxylase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006595biological_processpolyamine metabolic process
A0006596biological_processpolyamine biosynthetic process
A0008284biological_processpositive regulation of cell population proliferation
A0009446biological_processputrescine biosynthetic process
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
A0048471cellular_componentperinuclear region of cytoplasm
A1901605biological_processalpha-amino acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 425
ChainResidue
AGLY237
AGLU274
AGLY276
AARG277
ACYS360
ATYR389
AHOH686
AHOH724
AHOH744
AALA67
ALYS69
AASP88
AARG154
AHIS197
AGLY236

site_idCOF
Number of Residues1
DetailsK69 IS BOUND TO PLP VIA A SCHIFF BASE
ChainResidue
ALYS69

site_idDIN
Number of Residues1
DetailsDOMAIN INTERFACE
ChainResidue
AGLY387

site_idSSP
Number of Residues1
DetailsSUBSTRATE SPECIFICITY POCKET
ChainResidue
AASP361

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

site_idPS00879
Number of Residues18
DetailsODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. AtevgfsMhLLDIGGGFP
ChainResidueDetails
AALA222-PRO239

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":"10378276","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1730582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8504104","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P11926","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10378276","evidenceCode":"ECO:0000269"}]}
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":"PubMed","id":"10378276","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10378276","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1730582","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7ODC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P11926","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 10378276
ChainResidueDetails
AGLU274
ALYS69
AHIS197

site_idMCSA1
Number of Residues3
DetailsM-CSA 937
ChainResidueDetails
ALYS69
AHIS197
AGLU274

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PDB entries from 2025-10-08

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