eF-site ID 1w6c-A PDB Code 1w6c Chain A click to enlarge Title AGAO holoenzyme in a small cell, at 2.2 angstroms Classification OXIDOREDUCTASE Compound PHENYLETHYLAMINE OXIDASE Source (1W6C) Sequence A:  ASPFRLASAGEISEVQGILRTAGLLGPEKRIAYLGVLDPA RGAGSEAEDRRFRVFIHDVSGARPQEVTVSVTNGTVISAV ELDTAATGELPVLEEEFEVVEQLLATDERWLKALAARNLD VSKVRVAPLSAGVFEYAEERGRRILRGLAFVQDFPEDSAW AHPVDGLVAYVDVVSKEVTRVIDTGVFPVPAEHGNYTDPE LTGPLRTTQKPISITQPEGPSFTVTGGNHIEWEKWSLDVG FDVREGVVLHNIAFRDGDRLRPIINRASIAEMVVPYGDPS PIRSWQNYFDTGEYLVGQYANSLELGCDCLGDITYLSPVI SDAFGNPREIRNGICMHEEDWGILAKHSDLWSGINYTRRN RRMVISFFTTIGNXDYGFYWYLYLDGTIEFEAKATGVVFT SAFPEGGSDNISQLAPGLGAPFHQHIFSARLDMAIDGFTN RVEEEDVVRQTMGPGNERGNAFSRKRTVLTRESEAVREAD ARTGRTWIISNPESKNRLNEPVGYKLHAHNQPTLLADPGS SIARRAAFATKDLWVTRYADDERYPTGDFVNQHSGGAGLP SYIAQDRDIDGQDIVVWHTFGLTHFPRVEDWPIMPVDTVG FKLRPEGFFDRSPVLDVPAN Description Functional site 1) chain A residue 431 type sequence H description BINDING SITE FOR RESIDUE CU A 701 source : AC1 2) chain A residue 433 type sequence H description BINDING SITE FOR RESIDUE CU A 701 source : AC1 3) chain A residue 592 type sequence H description BINDING SITE FOR RESIDUE CU A 701 source : AC1 4) chain A residue 161 type sequence D description BINDING SITE FOR RESIDUE CU A 702 source : AC2 5) chain A residue 165 type sequence D description BINDING SITE FOR RESIDUE CU A 702 source : AC2 6) chain A residue 170 type sequence H description BINDING SITE FOR RESIDUE CU A 702 source : AC2 7) chain A residue 201 type sequence H description BINDING SITE FOR RESIDUE CU A 702 source : AC2 8) chain A residue 440 type sequence D description BINDING SITE FOR RESIDUE NA A 703 source : AC3 9) chain A residue 441 type sequence M description BINDING SITE FOR RESIDUE NA A 703 source : AC3 10) chain A residue 581 type sequence D description BINDING SITE FOR RESIDUE NA A 703 source : AC3 11) chain A residue 582 type sequence I description BINDING SITE FOR RESIDUE NA A 703 source : AC3 12) chain A residue 371-384 type prosite sequence MVISFFTTIGNXDY description COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. MVIsfftTigNYDY source prosite : PS01164 13) chain A residue 587-600 type prosite sequence TFGLTHFPRVEDWP description COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TfGltHFprvEDwP source prosite : PS01165 14) chain A residue 298 type ACT_SITE sequence D description Proton acceptor => ECO:0000250|UniProtKB:P12807 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 382 type ACT_SITE sequence X description Schiff-base intermediate with substrate; via topaquinone => ECO:0000250|UniProtKB:P12807 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 296 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P12807 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 379 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P46883 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 431 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9405045, ECO:0007744|PDB:1AV4, ECO:0007744|PDB:1AVL, ECO:0007744|PDB:1IU7, ECO:0007744|PDB:1IVU, ECO:0007744|PDB:1IVV, ECO:0007744|PDB:1IVW, ECO:0007744|PDB:1IVX, ECO:0007744|PDB:1RJO, ECO:0007744|PDB:1SIH, ECO:0007744|PDB:1SII, ECO:0007744|PDB:1UI8, ECO:0007744|PDB:1W4N, ECO:0007744|PDB:1W5Z, ECO:0007744|PDB:1W6C, ECO:0007744|PDB:1W6G, ECO:0007744|PDB:2BT3, ECO:0007744|PDB:2CFD, ECO:0007744|PDB:2CFG, ECO:0007744|PDB:2CFK, ECO:0007744|PDB:2CFL, ECO:0007744|PDB:2CFW, ECO:0007744|PDB:2CG0, ECO:0007744|PDB:2CG1, ECO:0007744|PDB:2CWT, ECO:0007744|PDB:2CWU, ECO:0007744|PDB:2CWV, ECO:0007744|PDB:2D1W, ECO:0007744|PDB:2E2T, ECO:0007744|PDB:2E2U, ECO:0007744|PDB:2E2V, ECO:0007744|PDB:2YX9, ECO:0007744|PDB:2ZL8, ECO:0007744|PDB:3AMO, ECO:0007744|PDB:3KII, ECO:0007744|PDB:3KN4, ECO:0007744|PDB:3WA2, ECO:0007744|PDB:3WA3 source Swiss-Prot : SWS_FT_FI5 19) chain A residue 433 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9405045, ECO:0007744|PDB:1AV4, ECO:0007744|PDB:1AVL, ECO:0007744|PDB:1IU7, ECO:0007744|PDB:1IVU, ECO:0007744|PDB:1IVV, ECO:0007744|PDB:1IVW, ECO:0007744|PDB:1IVX, ECO:0007744|PDB:1RJO, ECO:0007744|PDB:1SIH, ECO:0007744|PDB:1SII, ECO:0007744|PDB:1UI8, ECO:0007744|PDB:1W4N, ECO:0007744|PDB:1W5Z, ECO:0007744|PDB:1W6C, ECO:0007744|PDB:1W6G, ECO:0007744|PDB:2BT3, ECO:0007744|PDB:2CFD, ECO:0007744|PDB:2CFG, ECO:0007744|PDB:2CFK, ECO:0007744|PDB:2CFL, ECO:0007744|PDB:2CFW, ECO:0007744|PDB:2CG0, ECO:0007744|PDB:2CG1, ECO:0007744|PDB:2CWT, ECO:0007744|PDB:2CWU, ECO:0007744|PDB:2CWV, ECO:0007744|PDB:2D1W, ECO:0007744|PDB:2E2T, ECO:0007744|PDB:2E2U, ECO:0007744|PDB:2E2V, ECO:0007744|PDB:2YX9, ECO:0007744|PDB:2ZL8, ECO:0007744|PDB:3AMO, ECO:0007744|PDB:3KII, ECO:0007744|PDB:3KN4, ECO:0007744|PDB:3WA2, ECO:0007744|PDB:3WA3 source Swiss-Prot : SWS_FT_FI5 20) chain A residue 592 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9405045, ECO:0007744|PDB:1AV4, ECO:0007744|PDB:1AVL, ECO:0007744|PDB:1IU7, ECO:0007744|PDB:1IVU, ECO:0007744|PDB:1IVV, ECO:0007744|PDB:1IVW, ECO:0007744|PDB:1IVX, ECO:0007744|PDB:1RJO, ECO:0007744|PDB:1SIH, ECO:0007744|PDB:1SII, ECO:0007744|PDB:1UI8, ECO:0007744|PDB:1W4N, ECO:0007744|PDB:1W5Z, ECO:0007744|PDB:1W6C, ECO:0007744|PDB:1W6G, ECO:0007744|PDB:2BT3, ECO:0007744|PDB:2CFD, ECO:0007744|PDB:2CFG, ECO:0007744|PDB:2CFK, ECO:0007744|PDB:2CFL, ECO:0007744|PDB:2CFW, ECO:0007744|PDB:2CG0, ECO:0007744|PDB:2CG1, ECO:0007744|PDB:2CWT, ECO:0007744|PDB:2CWU, ECO:0007744|PDB:2CWV, ECO:0007744|PDB:2D1W, ECO:0007744|PDB:2E2T, ECO:0007744|PDB:2E2U, ECO:0007744|PDB:2E2V, ECO:0007744|PDB:2YX9, ECO:0007744|PDB:2ZL8, ECO:0007744|PDB:3AMO, ECO:0007744|PDB:3KII, ECO:0007744|PDB:3KN4, ECO:0007744|PDB:3WA2, ECO:0007744|PDB:3WA3 source Swiss-Prot : SWS_FT_FI5 21) chain A residue 382 type MOD_RES sequence X description 2',4',5'-topaquinone => ECO:0000269|PubMed:9405045 source Swiss-Prot : SWS_FT_FI6

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