|
eF-site ID
|
1ekm-A |
PDB Code
|
1ekm |
Chain
|
A |
|
click to enlarge
|
|
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
|
null (AMO_PICAN) |
|
Sequence
|
A: |
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 |
A |
residue |
405 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE ZN A 701
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
456 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 701
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
458 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 701
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
624 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 701
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
319 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000269|PubMed:9551552
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
6)
|
chain |
A |
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
|
|
7)
|
chain |
A |
residue |
317 |
type |
BINDING |
sequence |
A
|
description |
BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
8)
|
chain |
A |
residue |
402 |
type |
BINDING |
sequence |
A
|
description |
BINDING => ECO:0000250|UniProtKB:P46883
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
9)
|
chain |
A |
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 |
A |
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 |
A |
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
|
|
12)
|
chain |
A |
residue |
465 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250|UniProtKB:Q43077
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
13)
|
chain |
A |
residue |
613 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250|UniProtKB:Q43077
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
14)
|
chain |
A |
residue |
614 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000250|UniProtKB:Q43077
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
15)
|
chain |
A |
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
|
|
16)
|
chain |
A |
residue |
243 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
17)
|
chain |
A |
residue |
164-189 |
type |
prosite |
sequence |
WGTGKRLQQALVYYRSDEDDSQYSHP
|
description |
WW_DOMAIN_1 WW/rsp5/WWP domain signature. WgtgkrlqqalvYYrsdedd.SQYSHP
|
source |
prosite : PS01159
|
|
18)
|
chain |
A |
residue |
394-407 |
type |
prosite |
sequence |
LVVSQIFTAANYEY
|
description |
COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVsqifTaaNYEY
|
source |
prosite : PS01164
|
|
19)
|
chain |
A |
residue |
619-632 |
type |
prosite |
sequence |
TFGITHFPAPEDFP
|
description |
COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TfGitHFpapEDfP
|
source |
prosite : PS01165
|
|
|
|