eF-site ID 1ekm-ABC PDB Code 1ekm Chain A, B, C click to enlarge Title CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI Classification OXIDOREDUCTASE Compound COPPER AMINE OXIDASE Source Pichia angusta (Yeast) (Hansenula polymorpha) (AMO_PICAN) Sequence A:  APARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTL REPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLV DLASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIE QCVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVY YRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVS KHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTG NVMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRI SLSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGC DCKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKH SDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQD GAIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNH QHLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGN AFYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSG KPPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYK DNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILF FHTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLD IQPSYAMTTSEAKRAV B:  APARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTL REPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLV DLASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIE QCVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVY YRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVS KHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTG NVMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRI SLSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGC DCKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKH SDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQD GAIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNH QHLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGN AFYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSG KPPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYK DNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILF FHTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLD IQPSYAMTTSEAKRAV C:  APARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTL REPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLV DLASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIE QCVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVY YRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVS KHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTG NVMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRI SLSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGC DCKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKH SDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQD GAIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNH QHLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGN AFYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSG KPPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYK DNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILF FHTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLD IQPSYAMTTSEAKRAV Description (1)  COPPER AMINE OXIDASE (E.C.1.4.3.6) Functional site 1) chain A residue 405 type sequence Y description BINDING SITE FOR RESIDUE ZN A 701 source : AC1 2) chain A residue 456 type sequence H description BINDING SITE FOR RESIDUE ZN A 701 source : AC1 3) chain A residue 458 type sequence H description BINDING SITE FOR RESIDUE ZN A 701 source : AC1 4) chain A residue 624 type sequence H description BINDING SITE FOR RESIDUE ZN A 701 source : AC1 5) chain B residue 405 type sequence Y description BINDING SITE FOR RESIDUE ZN B 701 source : AC2 6) chain B residue 456 type sequence H description BINDING SITE FOR RESIDUE ZN B 701 source : AC2 7) chain B residue 458 type sequence H description BINDING SITE FOR RESIDUE ZN B 701 source : AC2 8) chain B residue 624 type sequence H description BINDING SITE FOR RESIDUE ZN B 701 source : AC2 9) chain C residue 405 type sequence Y description BINDING SITE FOR RESIDUE ZN C 701 source : AC3 10) chain C residue 456 type sequence H description BINDING SITE FOR RESIDUE ZN C 701 source : AC3 11) chain C residue 458 type sequence H description BINDING SITE FOR RESIDUE ZN C 701 source : AC3 12) chain C residue 624 type sequence H description BINDING SITE FOR RESIDUE ZN C 701 source : AC3 13) chain A residue 456 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI5 14) chain A residue 458 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI5 15) chain A residue 624 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI5 16) chain B residue 456 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI5 17) chain B residue 458 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI5 18) chain B residue 624 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI5 19) chain C residue 456 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI5 20) chain C residue 458 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI5 21) chain C residue 624 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI5 22) chain A residue 465 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 23) chain A residue 613 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 24) chain A residue 614 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 25) chain B residue 465 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 26) chain B residue 613 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 27) chain B residue 614 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 28) chain C residue 465 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 29) chain C residue 613 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 30) chain C residue 614 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 31) chain A residue 319 type ACT_SITE sequence D description Proton acceptor => ECO:0000269|PubMed:9551552 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 319 type ACT_SITE sequence D description Proton acceptor => ECO:0000269|PubMed:9551552 source Swiss-Prot : SWS_FT_FI1 33) chain C residue 319 type ACT_SITE sequence D description Proton acceptor => ECO:0000269|PubMed:9551552 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 405 type ACT_SITE sequence Y description Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI2 35) chain B residue 405 type ACT_SITE sequence Y description Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI2 36) chain C residue 405 type ACT_SITE sequence Y description Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI2 37) chain A residue 405 type MOD_RES sequence Y description 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE source Swiss-Prot : SWS_FT_FI7 38) chain B residue 405 type MOD_RES sequence Y description 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE source Swiss-Prot : SWS_FT_FI7 39) chain C residue 405 type MOD_RES sequence Y description 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE source Swiss-Prot : SWS_FT_FI7 40) chain A residue 243 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552 source Swiss-Prot : SWS_FT_FI8 41) chain B residue 243 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552 source Swiss-Prot : SWS_FT_FI8 42) chain C residue 243 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552 source Swiss-Prot : SWS_FT_FI8 43) chain A residue 164-189 type prosite sequence WGTGKRLQQALVYYRSDEDDSQYSHP description WW_DOMAIN_1 WW/rsp5/WWP domain signature. WgtgkrlqqalvYYrsdedd.SQYSHP source prosite : PS01159 44) chain A residue 394-407 type prosite sequence LVVSQIFTAANYEY description COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVsqifTaaNYEY source prosite : PS01164 45) chain A residue 619-632 type prosite sequence TFGITHFPAPEDFP description COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TfGitHFpapEDfP source prosite : PS01165 46) chain A residue 317 type BINDING sequence A description BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5 source Swiss-Prot : SWS_FT_FI3 47) chain B residue 317 type BINDING sequence A description BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5 source Swiss-Prot : SWS_FT_FI3 48) chain C residue 317 type BINDING sequence A description BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 402 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P46883 source Swiss-Prot : SWS_FT_FI4 50) chain B residue 402 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P46883 source Swiss-Prot : SWS_FT_FI4 51) chain C residue 402 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P46883 source Swiss-Prot : SWS_FT_FI4

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