eF-site ID 1a2v-ABCDEF
PDB Code 1a2v
Chain A, B, C, D, E, F
Title COPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA
Classification AMINE OXIDASE
Compound METHYLAMINE OXIDASE
Source null (AMO_PICAN)
Sequence A:  PARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLR
EPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLVD
LASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIEQ
CVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVYY
RSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSK
HKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGN
VMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRIS
LSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGCD
CKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKHS
DFRDNFATSLVTRATKLVVSQIFTAANXEYCLYWVFMQDG
AIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQ
HLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGNA
FYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSGK
PPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYKD
NRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILFF
HTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDI
QPSYAMTTSEAKRAV
B:  PARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLR
EPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLVD
LASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIEQ
CVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVYY
RSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSK
HKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGN
VMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRIS
LSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGCD
CKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKHS
DFRDNFATSLVTRATKLVVSQIFTAANXEYCLYWVFMQDG
AIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQ
HLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGNA
FYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSGK
PPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYKD
NRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILFF
HTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDI
QPSYAMTTSEAKRAV
C:  PARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLR
EPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLVD
LASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIEQ
CVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVYY
RSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSK
HKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGN
VMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRIS
LSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGCD
CKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKHS
DFRDNFATSLVTRATKLVVSQIFTAANXEYCLYWVFMQDG
AIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQ
HLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGNA
FYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSGK
PPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYKD
NRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILFF
HTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDI
QPSYAMTTSEAKRAV
D:  PARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLR
EPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLVD
LASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIEQ
CVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVYY
RSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSK
HKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGN
VMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRIS
LSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGCD
CKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKHS
DFRDNFATSLVTRATKLVVSQIFTAANXEYCLYWVFMQDG
AIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQ
HLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGNA
FYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSGK
PPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYKD
NRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILFF
HTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDI
QPSYAMTTSEAKRAV
E:  PARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLR
EPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLVD
LASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIEQ
CVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVYY
RSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSK
HKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGN
VMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRIS
LSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGCD
CKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKHS
DFRDNFATSLVTRATKLVVSQIFTAANXEYCLYWVFMQDG
AIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQ
HLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGNA
FYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSGK
PPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYKD
NRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILFF
HTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDI
QPSYAMTTSEAKRAV
F:  PARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLR
EPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLVD
LASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIEQ
CVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVYY
RSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSK
HKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGN
VMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRIS
LSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGCD
CKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKHS
DFRDNFATSLVTRATKLVVSQIFTAANXEYCLYWVFMQDG
AIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQ
HLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGNA
FYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSGK
PPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYKD
NRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILFF
HTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDI
QPSYAMTTSEAKRAV
Description


Functional site

1) chain A
residue 456
type
sequence H
description BINDING SITE FOR RESIDUE CU A 1
source : AC1

2) chain A
residue 458
type
sequence H
description BINDING SITE FOR RESIDUE CU A 1
source : AC1

3) chain A
residue 624
type
sequence H
description BINDING SITE FOR RESIDUE CU A 1
source : AC1

4) chain B
residue 456
type
sequence H
description BINDING SITE FOR RESIDUE CU B 1
source : AC2

5) chain B
residue 458
type
sequence H
description BINDING SITE FOR RESIDUE CU B 1
source : AC2

6) chain B
residue 624
type
sequence H
description BINDING SITE FOR RESIDUE CU B 1
source : AC2

7) chain C
residue 456
type
sequence H
description BINDING SITE FOR RESIDUE CU C 1
source : AC3

8) chain C
residue 458
type
sequence H
description BINDING SITE FOR RESIDUE CU C 1
source : AC3

9) chain C
residue 624
type
sequence H
description BINDING SITE FOR RESIDUE CU C 1
source : AC3

10) chain F
residue 456
type
sequence H
description BINDING SITE FOR RESIDUE CU D 1
source : AC4

11) chain F
residue 458
type
sequence H
description BINDING SITE FOR RESIDUE CU D 1
source : AC4

12) chain F
residue 624
type
sequence H
description BINDING SITE FOR RESIDUE CU D 1
source : AC4

13) chain E
residue 456
type
sequence H
description BINDING SITE FOR RESIDUE CU E 1
source : AC5

14) chain E
residue 458
type
sequence H
description BINDING SITE FOR RESIDUE CU E 1
source : AC5

15) chain E
residue 624
type
sequence H
description BINDING SITE FOR RESIDUE CU E 1
source : AC5

16) chain D
residue 456
type
sequence H
description BINDING SITE FOR RESIDUE CU F 1
source : AC6

17) chain D
residue 458
type
sequence H
description BINDING SITE FOR RESIDUE CU F 1
source : AC6

18) chain D
residue 624
type
sequence H
description BINDING SITE FOR RESIDUE CU F 1
source : AC6

19) chain B
residue 319
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000269|PubMed:9551552
source Swiss-Prot : SWS_FT_FI1

20) chain C
residue 319
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000269|PubMed:9551552
source Swiss-Prot : SWS_FT_FI1

21) chain D
residue 319
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000269|PubMed:9551552
source Swiss-Prot : SWS_FT_FI1

22) chain E
residue 319
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000269|PubMed:9551552
source Swiss-Prot : SWS_FT_FI1

23) chain F
residue 319
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000269|PubMed:9551552
source Swiss-Prot : SWS_FT_FI1

24) chain A
residue 319
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000269|PubMed:9551552
source Swiss-Prot : SWS_FT_FI1

25) chain B
residue 405
type ACT_SITE
sequence X
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

26) chain C
residue 405
type ACT_SITE
sequence X
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

27) chain D
residue 405
type ACT_SITE
sequence X
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

28) chain E
residue 405
type ACT_SITE
sequence X
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

29) chain F
residue 405
type ACT_SITE
sequence X
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

30) chain A
residue 405
type ACT_SITE
sequence X
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

31) chain B
residue 317
type BINDING
sequence A
description BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5
source Swiss-Prot : SWS_FT_FI3

32) chain C
residue 317
type BINDING
sequence A
description BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5
source Swiss-Prot : SWS_FT_FI3

33) chain D
residue 317
type BINDING
sequence A
description BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5
source Swiss-Prot : SWS_FT_FI3

34) chain E
residue 317
type BINDING
sequence A
description BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5
source Swiss-Prot : SWS_FT_FI3

35) chain F
residue 317
type BINDING
sequence A
description BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5
source Swiss-Prot : SWS_FT_FI3

36) chain A
residue 317
type BINDING
sequence A
description BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5
source Swiss-Prot : SWS_FT_FI3

37) chain C
residue 402
type BINDING
sequence A
description BINDING => ECO:0000250|UniProtKB:P46883
source Swiss-Prot : SWS_FT_FI4

38) chain D
residue 402
type BINDING
sequence A
description BINDING => ECO:0000250|UniProtKB:P46883
source Swiss-Prot : SWS_FT_FI4

39) chain E
residue 402
type BINDING
sequence A
description BINDING => ECO:0000250|UniProtKB:P46883
source Swiss-Prot : SWS_FT_FI4

40) chain F
residue 402
type BINDING
sequence A
description BINDING => ECO:0000250|UniProtKB:P46883
source Swiss-Prot : SWS_FT_FI4

41) chain A
residue 402
type BINDING
sequence A
description BINDING => ECO:0000250|UniProtKB:P46883
source Swiss-Prot : SWS_FT_FI4

42) chain B
residue 402
type BINDING
sequence A
description BINDING => ECO:0000250|UniProtKB:P46883
source Swiss-Prot : SWS_FT_FI4

43) 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

44) 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

45) 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

46) 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

47) chain D
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

48) chain D
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

49) chain D
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

50) chain E
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

51) chain E
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

52) chain E
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

53) chain F
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

54) chain F
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

55) chain F
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

56) 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

57) 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

58) 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

59) 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

60) 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

61) chain A
residue 613
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

62) chain A
residue 614
type BINDING
sequence I
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

63) chain B
residue 465
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

64) chain B
residue 613
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

65) chain B
residue 614
type BINDING
sequence I
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

66) chain D
residue 465
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

67) chain D
residue 613
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

68) chain D
residue 614
type BINDING
sequence I
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

69) chain E
residue 465
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

70) chain E
residue 613
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

71) chain E
residue 614
type BINDING
sequence I
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

72) chain F
residue 465
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

73) chain F
residue 613
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

74) chain F
residue 614
type BINDING
sequence I
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

75) chain C
residue 465
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

76) chain C
residue 613
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

77) chain C
residue 614
type BINDING
sequence I
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

78) chain A
residue 465
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6

79) chain B
residue 405
type MOD_RES
sequence X
description 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE
source Swiss-Prot : SWS_FT_FI7

80) chain C
residue 405
type MOD_RES
sequence X
description 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE
source Swiss-Prot : SWS_FT_FI7

81) chain D
residue 405
type MOD_RES
sequence X
description 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE
source Swiss-Prot : SWS_FT_FI7

82) chain E
residue 405
type MOD_RES
sequence X
description 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE
source Swiss-Prot : SWS_FT_FI7

83) chain F
residue 405
type MOD_RES
sequence X
description 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE
source Swiss-Prot : SWS_FT_FI7

84) chain A
residue 405
type MOD_RES
sequence X
description 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE
source Swiss-Prot : SWS_FT_FI7

85) chain B
residue 243
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552
source Swiss-Prot : SWS_FT_FI8

86) chain C
residue 243
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552
source Swiss-Prot : SWS_FT_FI8

87) chain D
residue 243
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552
source Swiss-Prot : SWS_FT_FI8

88) chain E
residue 243
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552
source Swiss-Prot : SWS_FT_FI8

89) chain F
residue 243
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552
source Swiss-Prot : SWS_FT_FI8

90) chain A
residue 243
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552
source Swiss-Prot : SWS_FT_FI8

91) chain A
residue 164-189
type prosite
sequence WGTGKRLQQALVYYRSDEDDSQYSHP
description WW_DOMAIN_1 WW/rsp5/WWP domain signature. WgtgkrlqqalvYYrsdedd.SQYSHP
source prosite : PS01159

92) chain A
residue 394-407
type prosite
sequence LVVSQIFTAANXEY
description COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVsqifTaaNYEY
source prosite : PS01164

93) 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


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