eF-site ID 1cqe-AB
PDB Code 1cqe
Chain A, B

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Title PROSTAGLANDIN H2 SYNTHASE-1 COMPLEX WITH FLURBIPROFEN
Classification OXIDOREDUCTASE
Compound PROTEIN (PROSTAGLANDIN H2 SYNTHASE-1)
Source ORGANISM_COMMON: sheep; ORGANISM_SCIENTIFIC: Ovis aries;
Sequence A:  PVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTI
PEIWTWLRTTLRPSPSFIHFLLTHGRWLWDFVNATFIRDT
LMRLVLTVRSNLIPSPPTYNIAHDYISWESFSNVSYYTRI
LPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDP
QGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLG
HIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPV
LMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHNR
VCDLLKAEHPTWGDEQLFQTARLILIGETIKIVIEEYVQQ
LSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLM
PDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPA
GRIGGGRNIDHHILHVAVDVIKESRVLRLQPFNEYRKRFG
MKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEK
CHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFG
GEVGFNLVKTATLKKLVCLNTKTCPYVSFHVP
B:  APVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCT
IPEIWTWLRTTLRPSPSFIHFLLTHGRWLWDFVNATFIRD
TLMRLVLTVRSNLIPSPPTYNIAHDYISWESFSNVSYYTR
ILPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPD
PQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDL
GHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAP
VLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHN
RVCDLLKAEHPTWGDEQLFQTARLILIGETIKIVIEEYVQ
QLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPL
MPDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQP
AGRIGGGRNIDHHILHVAVDVIKESRVLRLQPFNEYRKRF
GMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLE
KCHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTF
GGEVGFNLVKTATLKKLVCLNTKTCPYVSFHVP
Description


Functional site

1) chain A
residue 120
type
sequence R
description HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
source : COA

2) chain A
residue 355
type
sequence Y
description HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
source : COA

3) chain A
residue 385
type
sequence Y
description HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
source : COA

4) chain A
residue 387
type
sequence W
description HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
source : COA

5) chain A
residue 523
type
sequence I
description HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
source : COA

6) chain A
residue 530
type
sequence S
description HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
source : COA

7) chain B
residue 120
type
sequence R
description HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
source : COB

8) chain B
residue 355
type
sequence Y
description HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
source : COB

9) chain B
residue 385
type
sequence Y
description HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
source : COB

10) chain B
residue 387
type
sequence W
description HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
source : COB

11) chain B
residue 523
type
sequence I
description HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
source : COB

12) chain B
residue 530
type
sequence S
description HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
source : COB

13) chain A
residue 207
type
sequence H
description HEME POCKET RESPONSIBLE FOR PEROXIDASE ACTIVITY
source : POA

14) chain A
residue 388
type
sequence H
description HEME POCKET RESPONSIBLE FOR PEROXIDASE ACTIVITY
source : POA

15) chain B
residue 207
type
sequence H
description HEME POCKET RESPONSIBLE FOR PEROXIDASE ACTIVITY
source : POB

16) chain B
residue 388
type
sequence H
description HEME POCKET RESPONSIBLE FOR PEROXIDASE ACTIVITY
source : POB

17) chain A
residue 388
type BINDING
sequence H
description axial binding residue
source Swiss-Prot : SWS_FT_FI4

18) chain B
residue 388
type BINDING
sequence H
description axial binding residue
source Swiss-Prot : SWS_FT_FI4

19) chain A
residue 385
type ACT_SITE
sequence Y
description For cyclooxygenase activity => ECO:0000269|PubMed:2122967
source Swiss-Prot : SWS_FT_FI3

20) chain B
residue 385
type ACT_SITE
sequence Y
description For cyclooxygenase activity => ECO:0000269|PubMed:2122967
source Swiss-Prot : SWS_FT_FI3

21) chain A
residue 104
type SITE
sequence N
description Not glycosylated => ECO:0000269|PubMed:8349699
source Swiss-Prot : SWS_FT_FI5

22) chain B
residue 104
type SITE
sequence N
description Not glycosylated => ECO:0000269|PubMed:8349699
source Swiss-Prot : SWS_FT_FI5

23) chain A
residue 74-82
type TRANSMEM
sequence IWTWLRTTL
description Helical
source Swiss-Prot : SWS_FT_FI1

24) chain A
residue 86-92
type TRANSMEM
sequence PSFIHFL
description Helical
source Swiss-Prot : SWS_FT_FI1

25) chain A
residue 97-105
type TRANSMEM
sequence RWLWDFVNA
description Helical
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 108-122
type TRANSMEM
sequence IRDTLMRLVLTVRSN
description Helical
source Swiss-Prot : SWS_FT_FI1

27) chain B
residue 74-82
type TRANSMEM
sequence IWTWLRTTL
description Helical
source Swiss-Prot : SWS_FT_FI1

28) chain B
residue 86-92
type TRANSMEM
sequence PSFIHFL
description Helical
source Swiss-Prot : SWS_FT_FI1

29) chain B
residue 97-105
type TRANSMEM
sequence RWLWDFVNA
description Helical
source Swiss-Prot : SWS_FT_FI1

30) chain B
residue 108-122
type TRANSMEM
sequence IRDTLMRLVLTVRSN
description Helical
source Swiss-Prot : SWS_FT_FI1

31) chain A
residue 207
type ACT_SITE
sequence H
description Proton acceptor
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 207
type ACT_SITE
sequence H
description Proton acceptor
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 530
type SITE
sequence S
description Aspirin-acetylated serine
source Swiss-Prot : SWS_FT_FI6

34) chain B
residue 530
type SITE
sequence S
description Aspirin-acetylated serine
source Swiss-Prot : SWS_FT_FI6

35) chain A
residue 68
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8349699
source Swiss-Prot : SWS_FT_FI7

36) chain A
residue 144
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8349699
source Swiss-Prot : SWS_FT_FI7

37) chain A
residue 410
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8349699
source Swiss-Prot : SWS_FT_FI7

38) chain B
residue 68
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8349699
source Swiss-Prot : SWS_FT_FI7

39) chain B
residue 144
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8349699
source Swiss-Prot : SWS_FT_FI7

40) chain B
residue 410
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8349699
source Swiss-Prot : SWS_FT_FI7


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