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


Display surface

Download
Links