eF-site ID 2fqg-A
PDB Code 2fqg
Chain A

click to enlarge
Title Crystal Structures of E. coli Laccase CueO under different copper binding situations
Classification OXIDOREDUCTASE
Compound Blue copper oxidase cueO
Source Escherichia coli (strain K12) (CUEO_ECOLI)
Sequence A:  RPTLPIPDLLTTDARNRIQLTIGAGQSTFGGKTATTWGYN
GNLLGPAVKLQRGKAVTVDIYNQLTEETTLHWHGLEVPGE
VDGGPQGIIPPGGKRSVTLNVDQPAATCWFHPHQHGKTGR
QVAMGLAGLVVIEDDEILKLMLPKQWGIDDVPVIVQDKKF
SADGQIDYQLDVMTAAVGWFGDTLLTNGAIYPQHAAPRGW
LRLRLLNGCNARSLNFATSDNRPLYVIASDGGLLPEPVKV
SELPVLMGERFEVLVEVNDNKPFDLVTLPVSQMGMAIAPF
DKPHPVMRIQPIAISASGALPDTLSSLPALPSLEGLTVRK
LQLSMDPMLDMMGMQMLMEKYGDQAMAGMFDFHHANKING
QAFDMNKPMFAAAKGQYERWVISGVGDMMLHPFHIHGTQF
RILSENGKPPAAHRAGWKDTVKVEGNVSEVLVKFNHDAPK
EHAYMAHCHLLEHEDTGMMLGFTV
Description


Functional site

1) chain A
residue 442
type
sequence L
description BINDING SITE FOR RESIDUE CU A 601
source : AC1

2) chain A
residue 443
type
sequence H
description BINDING SITE FOR RESIDUE CU A 601
source : AC1

3) chain A
residue 500
type
sequence C
description BINDING SITE FOR RESIDUE CU A 601
source : AC1

4) chain A
residue 505
type
sequence H
description BINDING SITE FOR RESIDUE CU A 601
source : AC1

5) chain A
residue 510
type
sequence M
description BINDING SITE FOR RESIDUE CU A 601
source : AC1

6) chain A
residue 101
type
sequence H
description BINDING SITE FOR RESIDUE CU A 603
source : AC2

7) chain A
residue 103
type
sequence H
description BINDING SITE FOR RESIDUE CU A 603
source : AC2

8) chain A
residue 446
type
sequence H
description BINDING SITE FOR RESIDUE CU A 603
source : AC2

9) chain A
residue 448
type
sequence H
description BINDING SITE FOR RESIDUE CU A 603
source : AC2

10) chain A
residue 253
type
sequence P
description BINDING SITE FOR RESIDUE NA A 901
source : AC3

11) chain A
residue 255
type
sequence Y
description BINDING SITE FOR RESIDUE NA A 901
source : AC3

12) chain A
residue 286
type
sequence E
description BINDING SITE FOR RESIDUE NA A 901
source : AC3

13) chain A
residue 49
type
sequence Q
description BINDING SITE FOR RESIDUE NA A 902
source : AC4

14) chain A
residue 91
type
sequence Y
description BINDING SITE FOR RESIDUE NA A 902
source : AC4

15) chain A
residue 101
type
sequence H
description BINDING SITE FOR RESIDUE C2O A 602
source : AC5

16) chain A
residue 103
type
sequence H
description BINDING SITE FOR RESIDUE C2O A 602
source : AC5

17) chain A
residue 141
type
sequence H
description BINDING SITE FOR RESIDUE C2O A 602
source : AC5

18) chain A
residue 143
type
sequence H
description BINDING SITE FOR RESIDUE C2O A 602
source : AC5

19) chain A
residue 446
type
sequence H
description BINDING SITE FOR RESIDUE C2O A 602
source : AC5

20) chain A
residue 448
type
sequence H
description BINDING SITE FOR RESIDUE C2O A 602
source : AC5

21) chain A
residue 499
type
sequence H
description BINDING SITE FOR RESIDUE C2O A 602
source : AC5

22) chain A
residue 501
type
sequence H
description BINDING SITE FOR RESIDUE C2O A 602
source : AC5

23) chain A
residue 45
type
sequence R
description BINDING SITE FOR RESIDUE CIT A 701
source : AC6

24) chain A
residue 82
type
sequence R
description BINDING SITE FOR RESIDUE CIT A 701
source : AC6

25) chain A
residue 134
type
sequence P
description BINDING SITE FOR RESIDUE CIT A 701
source : AC6

26) chain A
residue 485
type
sequence K
description BINDING SITE FOR RESIDUE CIT A 701
source : AC6

27) chain A
residue 487
type
sequence N
description BINDING SITE FOR RESIDUE CIT A 701
source : AC6

28) chain A
residue 49
type
sequence Q
description BINDING SITE FOR RESIDUE PGE A 801
source : AC7

29) chain A
residue 93
type
sequence Q
description BINDING SITE FOR RESIDUE PGE A 801
source : AC7

30) chain A
residue 230
type
sequence W
description BINDING SITE FOR RESIDUE PGE A 801
source : AC7

31) chain A
residue 286
type
sequence E
description BINDING SITE FOR RESIDUE PGE A 801
source : AC7

32) chain A
residue 103
type BINDING
sequence H
description type 3 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 141
type BINDING
sequence H
description type 3 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
source Swiss-Prot : SWS_FT_FI2

34) chain A
residue 143
type BINDING
sequence H
description type 3 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
source Swiss-Prot : SWS_FT_FI2

35) chain A
residue 448
type BINDING
sequence H
description type 3 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
source Swiss-Prot : SWS_FT_FI2

36) chain A
residue 499
type BINDING
sequence H
description type 3 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
source Swiss-Prot : SWS_FT_FI2

37) chain A
residue 501
type BINDING
sequence H
description type 3 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
source Swiss-Prot : SWS_FT_FI2

38) chain A
residue 443
type BINDING
sequence H
description type 1 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
source Swiss-Prot : SWS_FT_FI3

39) chain A
residue 500
type BINDING
sequence C
description type 1 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
source Swiss-Prot : SWS_FT_FI3

40) chain A
residue 505
type BINDING
sequence H
description type 1 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
source Swiss-Prot : SWS_FT_FI3

41) chain A
residue 499-510
type prosite
sequence HCHLLEHEDTGM
description MULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHlleHedtGM
source prosite : PS00080

42) chain A
residue 101
type BINDING
sequence H
description type 2 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
source Swiss-Prot : SWS_FT_FI1

43) chain A
residue 446
type BINDING
sequence H
description type 2 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
source Swiss-Prot : SWS_FT_FI1


Display surface

Download
Links