eF-site ID 1ekm-C
PDB Code 1ekm
Chain C

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Title CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI
Classification OXIDOREDUCTASE
Compound COPPER AMINE OXIDASE
Source Pichia angusta (Yeast) (Hansenula polymorpha) (AMO_PICAN)
Sequence C:  APARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTL
REPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLV
DLASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIE
QCVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVY
YRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVS
KHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTG
NVMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRI
SLSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGC
DCKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKH
SDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQD
GAIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNH
QHLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGN
AFYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSG
KPPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYK
DNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILF
FHTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLD
IQPSYAMTTSEAKRAV
Description (1)  COPPER AMINE OXIDASE (E.C.1.4.3.6)


Functional site

1) chain C
residue 405
type
sequence Y
description BINDING SITE FOR RESIDUE ZN C 701
source : AC3

2) chain C
residue 456
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 701
source : AC3

3) chain C
residue 458
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 701
source : AC3

4) chain C
residue 624
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 701
source : AC3

5) 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

6) 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

7) 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

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

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

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

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

12) chain C
residue 405
type ACT_SITE
sequence Y
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

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

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

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

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


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