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