eF-site ID 5zch-ABCD PDB Code 5zch Chain A, B, C, D click to enlarge Title Crystal structure of OsPP2C50 I267W:OsPYL/RCAR3 with (+)-ABA Classification PLANT PROTEIN Compound Protein phosphatase 2C 50 Source (PYL3_ORYSJ) Sequence A:  APVWGCASTRGRSAEMEDASAAVPRFADVPVRLLASRRDL DALGLDADALRLPAHLFGVFDGHGGAEVANYCRERIHVVL SAALARLGKNLGEMGEVDMKEHWDDVFTKCFQRVDDEVSG RVTRVGEVRSEPVTAENVGSTAVVALVCSSHVVVANCGDS RIVLCRGKEPVALSIDHKPDRKDERARIEAQGGKVIQWNG YRVSGWLAMSRSIGDRYLKPFVIPKPEVMVVPRAKDDDCL ILASDGLWDVVSNEEACKVARRQILLSTDPAAQAAADYLM RLALKKGSEDNITVIVVDLKP B:  PVWGCASTRGRSAEMEDASAAVPRFADVPVRLLASRRDLD ALGLDADALRLPAHLFGVFDGHGGAEVANYCRERIHVVLS AALARLGKNLGEMGEVDMKEHWDDVFTKCFQRVDDEVSGR VTRVVGEVRSEPVTAENVGSTAVVALVCSSHVVVANCGDS RIVLCRGEPVALSIDHKPDRKDERARIEAQGGKVIQWNGY RVSGWLAMSRSIGDRYLKPFVIPKPEVMVVPRAKDDDCLI LASDGLWDVVSNEEACKVARRQILLSTDPAAQAAADYLMR LALKKGSEDNITVIVVDLK C:  HRHEPRDHQCSSAVAKHIKAPVHLVWSLVRRFDQPQLFKP FVSRCEMKGNIEIGSVREVNVKSGLPATRSTERLELLDDN EHILSVRFVGGDHRLKNYSSILTVHPEVIDGRPGTLVIES FVVDVPEGNTKDETCYFVEALLKCNLKSLAEVSERLV D:  VRRFHRHEPRDHQCSSAVAKHIKAPVHLVWSLVRRFDQPQ LFKPFVSRCEMKGNIEIGSVREVNVKSGLPATRSTERLEL LDDNEHILSVRFVGGDHRLKNYSSILTVHPEVIDGRPGTL VIESFVVDVPEGNTKDETCYFVEALLKCNLKSLAEVSERL VVK 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 75 type sequence D description binding site for residue MG A 402 source : AC2 5) chain A residue 118 type sequence D description binding site for residue MG A 402 source : AC2 6) chain A residue 119 type sequence G description binding site for residue MG A 402 source : AC2 7) chain C residue 76 type sequence K description binding site for residue A8S C 301 source : AC3 8) chain C residue 107 type sequence S description binding site for residue A8S C 301 source : AC3 9) chain C residue 125 type sequence F description binding site for residue A8S C 301 source : AC3 10) chain C residue 130 type sequence H description binding site for residue A8S C 301 source : AC3 11) chain C residue 174 type sequence F description binding site for residue A8S C 301 source : AC3 12) chain C residue 178 type sequence L description binding site for residue A8S C 301 source : AC3 13) chain C residue 179 type sequence L description binding site for residue A8S C 301 source : AC3 14) chain C residue 182 type sequence N description binding site for residue A8S C 301 source : AC3 15) chain B residue 118 type sequence D description binding site for residue MG B 401 source : AC4 16) chain B residue 119 type sequence G description binding site for residue MG B 401 source : AC4 17) chain B residue 118 type sequence D description binding site for residue MG B 402 source : AC5 18) chain B residue 306 type sequence D description binding site for residue MG B 402 source : AC5 19) chain B residue 368 type sequence D description binding site for residue MG B 402 source : AC5 20) chain D residue 76 type sequence K description binding site for residue A8S D 301 source : AC6 21) chain D residue 98 type sequence V description binding site for residue A8S D 301 source : AC6 22) chain D residue 107 type sequence S description binding site for residue A8S D 301 source : AC6 23) chain D residue 125 type sequence F description binding site for residue A8S D 301 source : AC6 24) chain D residue 130 type sequence H description binding site for residue A8S D 301 source : AC6 25) chain D residue 174 type sequence F description binding site for residue A8S D 301 source : AC6 26) chain D residue 178 type sequence L description binding site for residue A8S D 301 source : AC6 27) chain D residue 179 type sequence L description binding site for residue A8S D 301 source : AC6 28) chain D residue 182 type sequence N description binding site for residue A8S D 301 source : AC6 29) chain A residue 113-121 type prosite sequence LFGVFDGHG description PPM_1 PPM-type phosphatase domain signature. LFGVFDGHG source prosite : PS01032 30) chain C residue 76 type BINDING sequence K description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP source Swiss-Prot : SWS_FT_FI1 31) chain D residue 76 type BINDING sequence K description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP source Swiss-Prot : SWS_FT_FI1 32) chain A residue 306 type BINDING sequence D description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP source Swiss-Prot : SWS_FT_FI1 33) chain A residue 368 type BINDING sequence D description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP source Swiss-Prot : SWS_FT_FI1 34) chain B residue 118 type BINDING sequence D description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP source Swiss-Prot : SWS_FT_FI1 35) chain B residue 119 type BINDING sequence G description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP source Swiss-Prot : SWS_FT_FI1 36) chain B residue 306 type BINDING sequence D description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP source Swiss-Prot : SWS_FT_FI1 37) chain B residue 368 type BINDING sequence D description BINDING => ECO:0000269|PubMed:28827170, ECO:0007744|PDB:5GWP source Swiss-Prot : SWS_FT_FI1 38) chain C residue 104 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:O49686 source Swiss-Prot : SWS_FT_FI2 39) chain C residue 131 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:O49686 source Swiss-Prot : SWS_FT_FI2 40) chain C residue 156 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:O49686 source Swiss-Prot : SWS_FT_FI2 41) chain D residue 104 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:O49686 source Swiss-Prot : SWS_FT_FI2 42) chain D residue 131 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:O49686 source Swiss-Prot : SWS_FT_FI2 43) chain D residue 156 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:O49686 source Swiss-Prot : SWS_FT_FI2 44) chain C residue 77 type SITE sequence P description Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7 source Swiss-Prot : SWS_FT_FI3 45) chain C residue 175 type SITE sequence V description Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7 source Swiss-Prot : SWS_FT_FI3 46) chain D residue 77 type SITE sequence P description Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7 source Swiss-Prot : SWS_FT_FI3 47) chain D residue 175 type SITE sequence V description Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7 source Swiss-Prot : SWS_FT_FI3 48) chain C residue 103 type SITE sequence P description Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686 source Swiss-Prot : SWS_FT_FI4 49) chain C residue 167 type SITE sequence T description Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686 source Swiss-Prot : SWS_FT_FI4 50) chain D residue 103 type SITE sequence P description Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686 source Swiss-Prot : SWS_FT_FI4 51) 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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