eF-site ID 1qal-AB
PDB Code 1qal
Chain A, B

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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
B:  HMVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGA
QTAIVNGQPLALQVPVVMKDNKAWVSDTFINDVFQSGLDQ
TFQVEKRPHPLNALTADEIKQAVEIVKASADFKPNTRFTE
ISLLPPDKEAVWAFALENKPVDQPRKADVIMLDGKHIIEA
VVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEF
AAAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKV
ISYLDVGDGNYWAHPIENLVAVVDLEQKKIVKIEEGPVVP
VPMTARPFDGRDRVAPAVKPMQIIEPEGKNYTITGDMIHW
RNWDFHLSMNSRVGPMISTVTYNDNGTKRKVMYEGSLGGM
IVPYGDPDIGWYFKAYLNSGDYGMGTLTSPIARGKDAPSN
AVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQ
PNVSTERRELVVRWISTVGNXDYIFDWIFHENGTIGIDAG
ATGIEAVKGVKAKTMHDETAKDDTRYGTLIDHNIVGTTHQ
HIYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQV
NQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQI
IPYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHP
GERFPEGKYPNRSTHDTGLGQYSKDNESLDNTDAVVWMTT
GTTHVARAEEWPIMPTEWVHTLLKPWNFFDETPTLGALKK
D
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 B
residue 524
type
sequence H
description BINDING SITE FOR RESIDUE CU B 801
source : AC4
15) chain B
residue 526
type
sequence H
description BINDING SITE FOR RESIDUE CU B 801
source : AC4
16) chain B
residue 689
type
sequence H
description BINDING SITE FOR RESIDUE CU B 801
source : AC4
17) chain B
residue 133
type
sequence K
description BINDING SITE FOR RESIDUE CA B 802
source : AC5
18) chain B
residue 533
type
sequence D
description BINDING SITE FOR RESIDUE CA B 802
source : AC5
19) chain B
residue 534
type
sequence L
description BINDING SITE FOR RESIDUE CA B 802
source : AC5
20) chain B
residue 535
type
sequence D
description BINDING SITE FOR RESIDUE CA B 802
source : AC5
21) chain B
residue 678
type
sequence D
description BINDING SITE FOR RESIDUE CA B 802
source : AC5
22) chain B
residue 679
type
sequence A
description BINDING SITE FOR RESIDUE CA B 802
source : AC5
23) chain B
residue 573
type
sequence E
description BINDING SITE FOR RESIDUE CA B 803
source : AC6
24) chain B
residue 667
type
sequence Y
description BINDING SITE FOR RESIDUE CA B 803
source : AC6
25) chain B
residue 672
type
sequence E
description BINDING SITE FOR RESIDUE CA B 803
source : AC6
26) chain A
residue 369
type catalytic
sequence Y
description 864
source MCSA : MCSA1
27) chain A
residue 383
type catalytic
sequence N
description 864
source MCSA : MCSA1
28) chain A
residue 466
type catalytic
sequence X
description 864
source MCSA : MCSA1
29) chain A
residue 524
type catalytic
sequence H
description 864
source MCSA : MCSA1
30) chain A
residue 526
type catalytic
sequence H
description 864
source MCSA : MCSA1
31) chain A
residue 689
type catalytic
sequence H
description 864
source MCSA : MCSA1
32) chain B
residue 369
type catalytic
sequence Y
description 864
source MCSA : MCSA2
33) chain B
residue 383
type catalytic
sequence N
description 864
source MCSA : MCSA2
34) chain B
residue 466
type catalytic
sequence X
description 864
source MCSA : MCSA2
35) chain B
residue 524
type catalytic
sequence H
description 864
source MCSA : MCSA2
36) chain B
residue 526
type catalytic
sequence H
description 864
source MCSA : MCSA2
37) chain B
residue 689
type catalytic
sequence H
description 864
source MCSA : MCSA2
38) 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
39) chain B
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
40) chain A
residue 679
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI10
41) chain B
residue 679
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI10
42) chain A
residue 533
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6
43) chain A
residue 535
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6
44) chain A
residue 678
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6
45) chain B
residue 533
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6
46) chain B
residue 535
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6
47) chain B
residue 678
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q43077
source Swiss-Prot : SWS_FT_FI6
48) 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
49) chain B
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
50) 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
51) chain B
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
52) 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
53) chain B
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
54) 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
55) chain B
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
56) 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
57) chain B
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
58) 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
59) 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
60) 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
61) chain B
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
62) chain B
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
63) chain B
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
64) 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
65) chain B
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
66) 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
67) 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
68) 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
69) chain B
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
70) chain B
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
71) chain B
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
72) chain A
residue 455-468
type prosite
sequence LVVRWISTVGNXDY
description COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVrwisTvgNYDY
source prosite : PS01164
73) 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

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