eF-site ID 1a2v-B
PDB Code 1a2v
Chain B

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Title COPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA
Classification AMINE OXIDASE
Compound METHYLAMINE OXIDASE
Source Pichia angusta (Yeast) (Hansenula polymorpha) (AMO_PICAN)
Sequence B:  PARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLR
EPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLVD
LASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIEQ
CVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVYY
RSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSK
HKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGN
VMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRIS
LSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGCD
CKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKHS
DFRDNFATSLVTRATKLVVSQIFTAANXEYCLYWVFMQDG
AIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQ
HLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGNA
FYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSGK
PPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYKD
NRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILFF
HTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDI
QPSYAMTTSEAKRAV
Description


Functional site

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

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

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

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

5) 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

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

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

8) 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

9) 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

10) 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

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

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

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

14) 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

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


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