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4ZGY

STRUCTURE of HUMAN ORNITHINE DECARBOXYLASE IN COMPLEX WITH A C-TERMINAL FRAGMENT OF ANTIZYME

Functional Information from GO Data
ChainGOidnamespacecontents
A0001822biological_processkidney development
A0003824molecular_functioncatalytic activity
A0004586molecular_functionornithine decarboxylase activity
A0005515molecular_functionprotein binding
A0005575cellular_componentcellular_component
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 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 Residues11
Detailsbinding site for residue PLP A 501
ChainResidue
ALYS69
AMG502
BPHE192
AASP88
AALA111
AHIS197
AGLY237
AGLU274
AGLY276
AARG277
ATYR389

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 502
ChainResidue
APHE238
AGLY276
AARG277
ATYR278
APLP501

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
DetailsACT_SITE: Proton donor; shared with dimeric partner => ECO:0000305|PubMed:10623504
ChainResidueDetails
ACYS360

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17407445, ECO:0007744|PDB:2OO0
ChainResidueDetails
ASER200
AGLY237

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17407445, ECO:0000269|PubMed:26305948, ECO:0000269|PubMed:26443277, ECO:0007744|PDB:2OO0
ChainResidueDetails
AGLU274
ATYR389

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P07805
ChainResidueDetails
ATYR331

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P07805
ChainResidueDetails
AASP361

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates => ECO:0000250|UniProtKB:P00860
ChainResidueDetails
AHIS197

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:26305948, ECO:0000305|PubMed:17407445
ChainResidueDetails
ALYS69

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P00860
ChainResidueDetails
ASER303

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine; in inhibited form => ECO:0000305|PubMed:11461922
ChainResidueDetails
ACYS360

218853

PDB entries from 2024-04-24

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