eF-site ID 5gwp-ABCD
PDB Code 5gwp
Chain A, B, C, D

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Title Crystal structure of RCAR3:PP2C wild-type with (+)-ABA
Classification HYDROLASE/RECEPTOR
Compound Probable protein phosphatase 2C 50
Source Oryza sativa subsp. japonica (Rice) (K4N2F7_ORYSA)
Sequence A:  PVWGCASTRGRSAEMEDASAAVPRFADVPVRLLASRRDLD
ALGLDADALRLPAHLFGVFDGHGGAEVANYCRERIHVVLS
AALARLGKNLGEMGEVDMKEHWDDVFTKCFQRVDDEVSGR
VTRVVGEVRSEPVTAENVGSTAVVALVCSSHVVVANCGDS
RIVLCRGKEPVALSIDHKPDRKDERARIEAQGGKVIQWNG
YRVSGILAMSRSIGDRYLKPFVIPKPEVMVVPRAKDDDCL
ILASDGLWDVVSNEEACKVARRQILLWHKNNSTDPAAQAA
ADYLMRLALKKGSEDNITVIVVDLK
B:  PVWGCASTRGRSAEMEDASAAVPRFADVPVRLLASRRDLD
ALGLDADALRLPAHLFGVFDGHGGAEVANYCRERIHVVLS
AALARLGKNLGEDMKEHWDDVFTKCFQRVDDEVSGRVTRV
VNGEVRSEPVTAENVGSTAVVALVCSSHVVVANCGDSRIV
LCRGKEPVALSIDHKPDRKDERARIEAQGGKVIQWNGYRV
SGILAMSRSIGDRYLKPFVIPKPEVMVVPRAKDDDCLILA
SDGLWDVVSNEEACKVARRQILLWHKSTDPAAQAAADYLM
RLALKKGSEDNITVIVVDLKPRKKL
C:  RRFHRHEPRDHQCSSAVAKHIKAPVHLVWSLVRRFDQPQL
FKPFVSRCEMKGNIEIGSVREVNVKSGLPATRSTERLELL
DDNEHILSVRFVGGDHRLKNYSSILTVHPEVIDGRPGTLV
IESFVVDVPEGNTKDETCYFVEALLKCNLKSLAEVSERLV
V
D:  CSSAVAKHIKAPVHLVWSLVRRFDQPQLFKPFVSRCEMKG
NIEIGSVREVNVKSGLPATRSTERLELLDDNEHILSVRFV
GGDHRLKNYSSILTVHPEVIDGRPGTLVIESFVVDVPEGN
TKDETCYFVEALLKCNLKSLAEVSERLVV
Description


Functional site

1) chain A
residue 118
type
sequence D
description binding site for residue MG A 401
source : AC1

2) chain A
residue 306
type
sequence D
description binding site for residue MG A 401
source : AC1

3) chain A
residue 368
type
sequence D
description binding site for residue MG A 401
source : AC1

4) chain A
residue 306
type
sequence D
description binding site for residue MG A 402
source : AC2

5) chain A
residue 310
type
sequence D
description binding site for residue MG A 402
source : AC2

6) chain A
residue 118
type
sequence D
description binding site for residue MG A 403
source : AC3

7) chain A
residue 119
type
sequence G
description binding site for residue MG A 403
source : AC3

8) chain B
residue 118
type
sequence D
description binding site for residue MG B 401
source : AC4

9) chain B
residue 306
type
sequence D
description binding site for residue MG B 401
source : AC4

10) chain B
residue 368
type
sequence D
description binding site for residue MG B 401
source : AC4

11) chain B
residue 306
type
sequence D
description binding site for residue MG B 402
source : AC5

12) chain B
residue 310
type
sequence D
description binding site for residue MG B 402
source : AC5

13) chain B
residue 118
type
sequence D
description binding site for residue MG B 403
source : AC6

14) chain B
residue 119
type
sequence G
description binding site for residue MG B 403
source : AC6

15) chain C
residue 76
type
sequence K
description binding site for residue A8S C 301
source : AC7

16) chain C
residue 98
type
sequence V
description binding site for residue A8S C 301
source : AC7

17) chain C
residue 104
type
sequence A
description binding site for residue A8S C 301
source : AC7

18) chain C
residue 125
type
sequence F
description binding site for residue A8S C 301
source : AC7

19) chain C
residue 174
type
sequence F
description binding site for residue A8S C 301
source : AC7

20) chain C
residue 178
type
sequence L
description binding site for residue A8S C 301
source : AC7

21) chain C
residue 182
type
sequence N
description binding site for residue A8S C 301
source : AC7

22) chain D
residue 76
type
sequence K
description binding site for residue A8S D 301
source : AC8

23) chain D
residue 107
type
sequence S
description binding site for residue A8S D 301
source : AC8

24) chain D
residue 125
type
sequence F
description binding site for residue A8S D 301
source : AC8

25) chain D
residue 130
type
sequence H
description binding site for residue A8S D 301
source : AC8

26) chain D
residue 178
type
sequence L
description binding site for residue A8S D 301
source : AC8

27) chain D
residue 182
type
sequence N
description binding site for residue A8S D 301
source : AC8

28) chain A
residue 113-121
type prosite
sequence LFGVFDGHG
description PPM_1 PPM-type phosphatase domain signature. LFGVFDGHG
source prosite : PS01032

29) chain C
residue 76
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP
source Swiss-Prot : SWS_FT_FI1

30) chain D
residue 76
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP
source Swiss-Prot : SWS_FT_FI1

31) chain A
residue 306
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 368
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP
source Swiss-Prot : SWS_FT_FI1

33) chain B
residue 118
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP
source Swiss-Prot : SWS_FT_FI1

34) chain B
residue 119
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP
source Swiss-Prot : SWS_FT_FI1

35) chain B
residue 306
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP
source Swiss-Prot : SWS_FT_FI1

36) chain B
residue 368
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP
source Swiss-Prot : SWS_FT_FI1

37) chain C
residue 104
type BINDING
sequence A
description BINDING => ECO:0000250|UniProtKB:O49686
source Swiss-Prot : SWS_FT_FI2

38) chain C
residue 131
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:O49686
source Swiss-Prot : SWS_FT_FI2

39) chain C
residue 156
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:O49686
source Swiss-Prot : SWS_FT_FI2

40) chain D
residue 104
type BINDING
sequence A
description BINDING => ECO:0000250|UniProtKB:O49686
source Swiss-Prot : SWS_FT_FI2

41) chain D
residue 131
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:O49686
source Swiss-Prot : SWS_FT_FI2

42) chain D
residue 156
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:O49686
source Swiss-Prot : SWS_FT_FI2

43) chain C
residue 77
type SITE
sequence P
description Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7
source Swiss-Prot : SWS_FT_FI3

44) chain C
residue 175
type SITE
sequence V
description Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7
source Swiss-Prot : SWS_FT_FI3

45) chain D
residue 77
type SITE
sequence P
description Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7
source Swiss-Prot : SWS_FT_FI3

46) chain D
residue 175
type SITE
sequence V
description Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7
source Swiss-Prot : SWS_FT_FI3

47) chain C
residue 103
type SITE
sequence P
description Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686
source Swiss-Prot : SWS_FT_FI4

48) chain C
residue 167
type SITE
sequence T
description Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686
source Swiss-Prot : SWS_FT_FI4

49) chain D
residue 103
type SITE
sequence P
description Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686
source Swiss-Prot : SWS_FT_FI4

50) chain D
residue 167
type SITE
sequence T
description Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686
source Swiss-Prot : SWS_FT_FI4


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