eF-site ID 3nmv-B PDB Code 3nmv Chain B click to enlarge Title Crystal structure of pyrabactin-bound abscisic acid receptor PYL2 mutant A93F in complex with type 2C protein phosphatase ABI2 Classification PROTEIN BINDING Compound Abscisic acid receptor PYL2 Source Arabidopsis thaliana (Mouse-ear cress) (P2C77_ARATH) Sequence B:  CVPLYGVTSICGRRPEMEDSVSTIPRFLQNGFNPHLSAHF FGVYDGHGGSQVANYCRERMHLALTEEIVKEKPEFCDGDT WQEKWKKALFNSFMRVDSEIETVAHAPETVGSTSVVAVVF PTHIFVANCGDSRAVLCRGKTPLALSVDHKPDRDDEAARI EAAGGKVIRWNGARVFGVLAMSRSIGDRYLKPSVIPDPEV TSVRRVKEDDCLILASDGLWDVMTNEEVCDLARKRILLWH KKNEGKDPAAMSAAEYLSKMALQKGSKDNISVVVVDLKGI Description Functional site 1) chain B residue 127 type sequence D description BINDING SITE FOR RESIDUE MG B 424 source : AC2 2) chain B residue 165 type sequence D description BINDING SITE FOR RESIDUE MG B 424 source : AC2 3) chain B residue 337 type sequence D description BINDING SITE FOR RESIDUE MG B 424 source : AC2 4) chain B residue 402 type sequence D description BINDING SITE FOR RESIDUE MG B 424 source : AC2 5) chain B residue 403 type sequence N description BINDING SITE FOR RESIDUE MG B 424 source : AC2 6) chain B residue 165 type sequence D description BINDING SITE FOR RESIDUE MG B 425 source : AC3 7) chain B residue 251 type sequence D description BINDING SITE FOR RESIDUE MG B 425 source : AC3 8) chain B residue 252 type sequence S description BINDING SITE FOR RESIDUE MG B 425 source : AC3 9) chain B residue 336 type sequence S description BINDING SITE FOR RESIDUE MG B 425 source : AC3 10) chain B residue 337 type sequence D description BINDING SITE FOR RESIDUE MG B 425 source : AC3 11) chain B residue 126 type sequence E description BINDING SITE FOR RESIDUE MG B 426 source : AC4 12) chain B residue 166 type sequence G description BINDING SITE FOR RESIDUE MG B 426 source : AC4 13) chain B residue 160-168 type prosite sequence FFGVYDGHG description PPM_1 PPM-type phosphatase domain signature. FFGVYDGHG source prosite : PS01032 14) chain B residue 290 type SITE sequence W description Lock => ECO:0000250|UniProtKB:Q9CAJ0 source Swiss-Prot : SWS_FT_FI3 15) chain B residue 165 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJK, ECO:0007744|PDB:3UJL source Swiss-Prot : SWS_FT_FI1 16) chain B residue 337 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJK, ECO:0007744|PDB:3UJL source Swiss-Prot : SWS_FT_FI1 17) chain B residue 402 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJK, ECO:0007744|PDB:3UJL source Swiss-Prot : SWS_FT_FI1 18) chain B residue 251 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJL source Swiss-Prot : SWS_FT_FI2 19) chain B residue 252 type BINDING sequence S description BINDING => ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJL source Swiss-Prot : SWS_FT_FI2

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