eF-site ID 1b4v-A
PDB Code 1b4v
Chain A

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Title CHOLESTEROL OXIDASE FROM STREPTOMYCES
Classification OXIDOREDUCTASE
Compound PROTEIN (CHOLESTEROL OXIDASE)
Source ORGANISM_SCIENTIFIC: Streptomyces sp.;
Sequence A:  GYVPAVVIGTGYGAAVSALRLGEAGVQTLMLEMGQLWNQP
GPDGNIFCGMLNPDKRSSWFKNRTEAPLGSFLWLDVVNRN
IDPYAGVLDRVNYDQMSVYVGRGVGGGSLVNGGMAVEPKR
SYFEEILPRVDSSEMYDRYFPRANSMLRVNHIDTKWFEDT
EWYKFARVSREQAGKAGLGTVFVPNVYDFGYMQREAAGEV
PKSALATEVIYGNNHGKQSLDKTYLAAALGTGKVTIQTLH
QVKTIRQTKDGGYALTVEQKDTDGKLLATKEISCRYLFLG
AGSLGSTELLVRARDTGTLPNLNSEVGAGWGPNGNIMTAR
ANHMWNPTGAHQSSIPALGIDAWDNSDSSVFAEIAPMPAG
LETWVSLYLAITKNPQRGTFVYDAATDRAKLNWTRDQNAP
AVNAAKALFDRINKANGTIYRYDLFGTQLKAFADDFCYHP
LGGCVLGKATDDYGRVAGYKNLYVTDGSLIPGSVGVNPFV
TITALAERNVERIIKQDV
Description


Functional site

1) chain A
residue 447
type
sequence H
description HISTIDINE 447 IS PRESUMED TO BE THE ACTIVE SITE BASE IN THE OXIDASE REACTION. THE BASE CATALYZED MECHANISM IS MEDIATED THROUGH A WATER MOLECULE AT POSITION 541. GLU 361 IS THE BASE IN THE ISOMERIZATION REACTION. ASN 485 IS BELIEVED TO BE INVOLVED IN POSITIONING THE WATER MOLECULE.
source : CAT

2) chain A
residue 361
type
sequence E
description HISTIDINE 447 IS PRESUMED TO BE THE ACTIVE SITE BASE IN THE OXIDASE REACTION. THE BASE CATALYZED MECHANISM IS MEDIATED THROUGH A WATER MOLECULE AT POSITION 541. GLU 361 IS THE BASE IN THE ISOMERIZATION REACTION. ASN 485 IS BELIEVED TO BE INVOLVED IN POSITIONING THE WATER MOLECULE.
source : CAT

3) chain A
residue 485
type
sequence N
description HISTIDINE 447 IS PRESUMED TO BE THE ACTIVE SITE BASE IN THE OXIDASE REACTION. THE BASE CATALYZED MECHANISM IS MEDIATED THROUGH A WATER MOLECULE AT POSITION 541. GLU 361 IS THE BASE IN THE ISOMERIZATION REACTION. ASN 485 IS BELIEVED TO BE INVOLVED IN POSITIONING THE WATER MOLECULE.
source : CAT

4) chain A
residue 16
type
sequence I
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

5) chain A
residue 17
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

6) chain A
residue 19
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

7) chain A
residue 20
type
sequence Y
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

8) chain A
residue 21
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

9) chain A
residue 39
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

10) chain A
residue 40
type
sequence E
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

11) chain A
residue 41
type
sequence M
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

12) chain A
residue 107
type
sequence Y
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

13) chain A
residue 109
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

14) chain A
residue 110
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

15) chain A
residue 111
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

16) chain A
residue 114
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

17) chain A
residue 115
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

18) chain A
residue 119
type
sequence N
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

19) chain A
residue 120
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

20) chain A
residue 121
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

21) chain A
residue 122
type
sequence M
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

22) chain A
residue 218
type
sequence I
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

23) chain A
residue 248
type
sequence H
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

24) chain A
residue 249
type
sequence Q
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

25) chain A
residue 250
type
sequence V
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

26) chain A
residue 288
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

27) chain A
residue 289
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

28) chain A
residue 290
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

29) chain A
residue 446
type
sequence Y
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

30) chain A
residue 447
type
sequence H
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

31) chain A
residue 474
type
sequence D
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

32) chain A
residue 475
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

33) chain A
residue 485
type
sequence N
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

34) chain A
residue 486
type
sequence P
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

35) chain A
residue 487
type
sequence F
description BINDING SITE FOR RESIDUE FAD A 510
source : AC1

36) chain A
residue 109-132
type prosite
sequence GRGVGGGSLVNGGMAVEPKRSYFE
description GMC_OXRED_1 GMC oxidoreductases signature 1. GRgVGGGSlVNggmAvePkrsyfE
source prosite : PS00623

37) chain A
residue 361
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:10194345
source Swiss-Prot : SWS_FT_FI1

38) chain A
residue 447
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000305|PubMed:10194345
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 20
type BINDING
sequence Y
description BINDING => ECO:0007744|PDB:1B4V
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 40
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:1B4V
source Swiss-Prot : SWS_FT_FI2

41) chain A
residue 115
type BINDING
sequence G
description BINDING => ECO:0007744|PDB:1B4V
source Swiss-Prot : SWS_FT_FI2

42) chain A
residue 119
type BINDING
sequence N
description BINDING => ECO:0007744|PDB:1B4V
source Swiss-Prot : SWS_FT_FI2

43) chain A
residue 250
type BINDING
sequence V
description BINDING => ECO:0007744|PDB:1B4V
source Swiss-Prot : SWS_FT_FI2

44) chain A
residue 475
type BINDING
sequence G
description BINDING => ECO:0007744|PDB:1B4V
source Swiss-Prot : SWS_FT_FI2

45) chain A
residue 487
type BINDING
sequence F
description BINDING => ECO:0007744|PDB:1B4V
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 446
type BINDING
sequence Y
description BINDING => ECO:0007744|PDB:1IJH
source Swiss-Prot : SWS_FT_FI3


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