eF-site ID 1qal-A PDB Code 1qal Chain A click to enlarge Title THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE : X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS Classification OXIDOREDUCTASE Compound COPPER AMINE OXIDASE Source Escherichia coli (strain K12) (AMO_ECOLI) Sequence A:  MVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQ TAIVNGQPLALQVPVVMKDNKAWVSDTFINDVFQSGLDQT FQVEKRPHPLNALTADEIKQAVEIVKASADFKPNTRFTEI SLLPPDKEAVWAFALENKPVDQPRKADVIMLDGKHIIEAV VDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFA AAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVI SYLDVGDGNYWAHPIENLVAVVDLEQKKIVKIEEGPVVPV PMTARPFDGRDRVAPAVKPMQIIEPEGKNYTITGDMIHWR NWDFHLSMNSRVGPMISTVTYNDNGTKRKVMYEGSLGGMI VPYGDPDIGWYFKAYLNSGDYGMGTLTSPIARGKDAPSNA VLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQP NVSTERRELVVRWISTVGNXDYIFDWIFHENGTIGIDAGA TGIEAVKGVKAKTMHDETAKDDTRYGTLIDHNIVGTTHQH IYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQVN QYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQII PYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPG ERFPEGKYPNRSTHDTGLGQYSKDNESLDNTDAVVWMTTG TTHVARAEEWPIMPTEWVHTLLKPWNFFDETPTLGALKK Description Functional site 1) chain A residue 524 type sequence H description BINDING SITE FOR RESIDUE CU A 801 source : AC1 2) chain A residue 526 type sequence H description BINDING SITE FOR RESIDUE CU A 801 source : AC1 3) chain A residue 689 type sequence H description BINDING SITE FOR RESIDUE CU A 801 source : AC1 4) chain A residue 133 type sequence K description BINDING SITE FOR RESIDUE CA A 802 source : AC2 5) chain A residue 533 type sequence D description BINDING SITE FOR RESIDUE CA A 802 source : AC2 6) chain A residue 534 type sequence L description BINDING SITE FOR RESIDUE CA A 802 source : AC2 7) chain A residue 535 type sequence D description BINDING SITE FOR RESIDUE CA A 802 source : AC2 8) chain A residue 678 type sequence D description BINDING SITE FOR RESIDUE CA A 802 source : AC2 9) chain A residue 679 type sequence A description BINDING SITE FOR RESIDUE CA A 802 source : AC2 10) chain A residue 573 type sequence E description BINDING SITE FOR RESIDUE CA A 803 source : AC3 11) chain A residue 667 type sequence Y description BINDING SITE FOR RESIDUE CA A 803 source : AC3 12) chain A residue 670 type sequence D description BINDING SITE FOR RESIDUE CA A 803 source : AC3 13) chain A residue 672 type sequence E description BINDING SITE FOR RESIDUE CA A 803 source : AC3 14) chain A residue 369 type catalytic sequence Y description 864 source MCSA : MCSA1 15) chain A residue 383 type catalytic sequence N description 864 source MCSA : MCSA1 16) chain A residue 466 type catalytic sequence X description 864 source MCSA : MCSA1 17) chain A residue 524 type catalytic sequence H description 864 source MCSA : MCSA1 18) chain A residue 526 type catalytic sequence H description 864 source MCSA : MCSA1 19) chain A residue 689 type catalytic sequence H description 864 source MCSA : MCSA1 20) chain A residue 455-468 type prosite sequence LVVRWISTVGNXDY description COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVrwisTvgNYDY source prosite : PS01164 21) chain A residue 684-697 type prosite sequence TTGTTHVARAEEWP description COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TtGttHVaraEEwP source prosite : PS01165 22) chain A residue 383 type ACT_SITE sequence N description Proton acceptor => ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1OAC source Swiss-Prot : SWS_FT_FI1 23) chain A residue 679 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI10 24) chain A residue 466 type MOD_RES sequence X description 2',4',5'-topaquinone => ECO:0000269|PubMed:10387067, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1QAF, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL source Swiss-Prot : SWS_FT_FI11 25) chain A residue 466 type ACT_SITE sequence X description Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:10387067, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WO0, ECO:0007744|PDB:2WOF source Swiss-Prot : SWS_FT_FI2 26) chain A residue 381 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10576737, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z source Swiss-Prot : SWS_FT_FI3 27) chain A residue 463 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1LVN, ECO:0007744|PDB:1SPU source Swiss-Prot : SWS_FT_FI4 28) chain A residue 524 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL, ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q, ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WO0, ECO:0007744|PDB:2WOF, ECO:0007744|PDB:2WOH source Swiss-Prot : SWS_FT_FI5 29) chain A residue 526 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL, ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q, ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WO0, ECO:0007744|PDB:2WOF, ECO:0007744|PDB:2WOH source Swiss-Prot : SWS_FT_FI5 30) chain A residue 689 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL, ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q, ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WO0, ECO:0007744|PDB:2WOF, ECO:0007744|PDB:2WOH source Swiss-Prot : SWS_FT_FI5 31) chain A residue 533 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 32) chain A residue 535 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 33) chain A residue 678 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 34) chain A residue 534 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL, ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q, ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WOH source Swiss-Prot : SWS_FT_FI7 35) chain A residue 573 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL, ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q, ECO:0007744|PDB:2WGQ source Swiss-Prot : SWS_FT_FI8 36) chain A residue 667 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL, ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q, ECO:0007744|PDB:2WGQ source Swiss-Prot : SWS_FT_FI8 37) chain A residue 672 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL, ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q, ECO:0007744|PDB:2WGQ source Swiss-Prot : SWS_FT_FI8 38) chain A residue 670 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10576737, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL, ECO:0007744|PDB:2WGQ source Swiss-Prot : SWS_FT_FI9

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