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

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Title Crystal structure of topaquinone-containing amine oxidase activated by cobalt ion
Classification OXIDOREDUCTASE
Compound Phenylethylamine oxidase
Source Arthrobacter globiformis (PAOX_ARTGO)
Sequence A:  ASPFRLASAGEISEVQGILRTAGLLGPEKRIAYLGVLDPA
RGAGSEAEDRRFRVFIHDVSGARPQEVTVSVTNGTVISAV
ELDTAATGELPVLEEEFEVVEQLLATDERWLKALAARNLD
VSKVRVAPLSAGVFEYAEERGRRILRGLAFVQDFPEDSAW
AHPVDGLVAYVDVVSKEVTRVIDTGVFPVPAEHGNYTDPE
LTGPLRTTQKPISITQPEGPSFTVTGGNHIEWEKWSLDVG
FDVREGVVLHNIAFRDGDRLRPIINRASIAEMVVPYGDPS
PIRSWQNYFDTGEYLVGQYANSLELGCDCLGDITYLSPVI
SDAFGNPREIRNGICMHEEDWGILAKHSDLWSGINYTRRN
RRMVISFFTTIGNXDYGFYWYLYLDGTIEFEAKATGVVFT
SAFPEGGSDNISQLAPGLGAPFHQHIFSARLDMAIDGFTN
RVEEEDVVRQTMGPGNERGNAFSRKRTVLTRESEAVREAD
ARTGRTWIISNPESKNRLNEPVGYKLHAHNQPTLLADPGS
SIARRAAFATKDLWVTRYADDERYPTGDFVNQHSGGAGLP
SYIAQDRDIDGQDIVVWHTFGLTHFPRVEDWPIMPVDTVG
FKLRPEGFFDRSPVLDVPAN
B:  ASPFRLASAGEISEVQGILRTAGLLGPEKRIAYLGVLDPA
RGAGSEAEDRRFRVFIHDVSGARPQEVTVSVTNGTVISAV
ELDTAATGELPVLEEEFEVVEQLLATDERWLKALAARNLD
VSKVRVAPLSAGVFEYAEERGRRILRGLAFVQDFPEDSAW
AHPVDGLVAYVDVVSKEVTRVIDTGVFPVPAEHGNYTDPE
LTGPLRTTQKPISITQPEGPSFTVTGGNHIEWEKWSLDVG
FDVREGVVLHNIAFRDGDRLRPIINRASIAEMVVPYGDPS
PIRSWQNYFDTGEYLVGQYANSLELGCDCLGDITYLSPVI
SDAFGNPREIRNGICMHEEDWGILAKHSDLWSGINYTRRN
RRMVISFFTTIGNXDYGFYWYLYLDGTIEFEAKATGVVFT
SAFPEGGSDNISQLAPGLGAPFHQHIFSARLDMAIDGFTN
RVEEEDVVRQTMGPGNERGNAFSRKRTVLTRESEAVREAD
ARTGRTWIISNPESKNRLNEPVGYKLHAHNQPTLLADPGS
SIARRAAFATKDLWVTRYADDERYPTGDFVNQHSGGAGLP
SYIAQDRDIDGQDIVVWHTFGLTHFPRVEDWPIMPVDTVG
FKLRPEGFFDRSPVLDVPAN
Description (1)  Phenylethylamine oxidase (E.C.1.4.3.6)


Functional site
1) chain A
residue 431
type
sequence H
description BINDING SITE FOR RESIDUE CO A 1001
source : AC1
2) chain A
residue 433
type
sequence H
description BINDING SITE FOR RESIDUE CO A 1001
source : AC1
3) chain A
residue 592
type
sequence H
description BINDING SITE FOR RESIDUE CO A 1001
source : AC1
4) chain B
residue 431
type
sequence H
description BINDING SITE FOR RESIDUE CO B 1002
source : AC2
5) chain B
residue 433
type
sequence H
description BINDING SITE FOR RESIDUE CO B 1002
source : AC2
6) chain B
residue 592
type
sequence H
description BINDING SITE FOR RESIDUE CO B 1002
source : AC2
7) chain A
residue 298
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000250|UniProtKB:P12807
source Swiss-Prot : SWS_FT_FI1
8) chain B
residue 298
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000250|UniProtKB:P12807
source Swiss-Prot : SWS_FT_FI1
9) 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
10) chain B
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
11) chain A
residue 296
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P12807
source Swiss-Prot : SWS_FT_FI3
12) chain B
residue 296
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P12807
source Swiss-Prot : SWS_FT_FI3
13) chain A
residue 379
type BINDING
sequence I
description BINDING => ECO:0000250|UniProtKB:P46883
source Swiss-Prot : SWS_FT_FI4
14) chain B
residue 379
type BINDING
sequence I
description BINDING => ECO:0000250|UniProtKB:P46883
source Swiss-Prot : SWS_FT_FI4
15) chain A
residue 371-384
type prosite
sequence MVISFFTTIGNXDY
description COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. MVIsfftTigNYDY
source prosite : PS01164
16) 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
17) chain A
residue 382
type MOD_RES
sequence X
description 2',4',5'-topaquinone => ECO:0000269|PubMed:9405045
source Swiss-Prot : SWS_FT_FI6
18) chain B
residue 382
type MOD_RES
sequence X
description 2',4',5'-topaquinone => ECO:0000269|PubMed:9405045
source Swiss-Prot : SWS_FT_FI6
19) 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
20) 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
21) 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
22) chain B
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
23) chain B
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
24) chain B
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

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