eF-site ID 4zgy-A PDB Code 4zgy Chain A click to enlarge Title STRUCTURE of HUMAN ORNITHINE DECARBOXYLASE IN COMPLEX WITH A C-TERMINAL FRAGMENT OF ANTIZYME Classification LYASE/LYASE INHIBITOR Compound Ornithine decarboxylase Source Homo sapiens (Human) (OAZ1_HUMAN) Sequence A:  TAKDILDQKINEKDAFYVADLGDILKKHLRWLKALPRVTP FYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVP PERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVAR AHPKAKLVLRIATDDSCRLSVKFGATLRTSRLLLERAKEL NIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGF SMYLLDIGGGFPGSEDVKLKFEEITGVINPALDKYFPSDS GVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSSEQT FMYYVNDGVYGSFNCILYDHAHVKPLLQKRPEKYYSSSIW GPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVASTFN GFQRPTIYYVMSGPAWQLMQQFQ Description Functional site 1) chain A residue 69 type sequence K description binding site for residue PLP A 501 source : AC1 2) chain A residue 88 type sequence D description binding site for residue PLP A 501 source : AC1 3) chain A residue 111 type sequence A description binding site for residue PLP A 501 source : AC1 4) chain A residue 197 type sequence H description binding site for residue PLP A 501 source : AC1 5) chain A residue 237 type sequence G description binding site for residue PLP A 501 source : AC1 6) chain A residue 274 type sequence E description binding site for residue PLP A 501 source : AC1 7) chain A residue 276 type sequence G description binding site for residue PLP A 501 source : AC1 8) chain A residue 277 type sequence R description binding site for residue PLP A 501 source : AC1 9) chain A residue 389 type sequence Y description binding site for residue PLP A 501 source : AC1 10) chain A residue 238 type sequence F description binding site for residue MG A 502 source : AC2 11) chain A residue 276 type sequence G description binding site for residue MG A 502 source : AC2 12) chain A residue 277 type sequence R description binding site for residue MG A 502 source : AC2 13) chain A residue 278 type sequence Y description binding site for residue MG A 502 source : AC2 14) chain A residue 360 type MOD_RES sequence C description S-nitrosocysteine; in inhibited form => ECO:0000305|PubMed:11461922 source Swiss-Prot : SWS_FT_FI9 15) chain A residue 200 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17407445, ECO:0007744|PDB:2OO0 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 237 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17407445, ECO:0007744|PDB:2OO0 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 360 type ACT_SITE sequence C description Proton donor; shared with dimeric partner => ECO:0000305|PubMed:10623504 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 66-84 type prosite sequence YAVKCNDSKAIVKTLAATG description ODR_DC_2_1 Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site. YAvKCNdskaIVktLaatG source prosite : PS00878 19) chain A residue 222-239 type prosite sequence GAEVGFSMYLLDIGGGFP description ODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. GaevgfsMyLLDIGGGFP source prosite : PS00879 20) chain A residue 197 type SITE sequence H description Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates => ECO:0000250|UniProtKB:P00860 source Swiss-Prot : SWS_FT_FI6 21) chain A residue 69 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:26305948, ECO:0000305|PubMed:17407445 source Swiss-Prot : SWS_FT_FI7 22) chain A residue 274 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17407445, ECO:0000269|PubMed:26305948, ECO:0000269|PubMed:26443277, ECO:0007744|PDB:2OO0 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 389 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17407445, ECO:0000269|PubMed:26305948, ECO:0000269|PubMed:26443277, ECO:0007744|PDB:2OO0 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 331 type BINDING sequence Y description in other chain => ECO:0000250|UniProtKB:P07805 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 361 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P07805 source Swiss-Prot : SWS_FT_FI5

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