eF-site ID 4ja9-A PDB Code 4ja9 Chain A click to enlarge Title Rat PP5 apo Classification HYDROLASE Compound Serine/threonine-protein phosphatase 5 Source Rattus norvegicus (Rat) (PPP5_RAT) Sequence A:  GTLKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNA IYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRR AASNMALGKFRAALRDYETVVKVKPNDKDAKMKYQECSKI VKQKAFERSVVDSLDIESMTIEDEYSGPKLEDGKVTITFM KDLMQWYKDQKKLHRKCAYQILVQVKEVLCKLSTLVETTL KETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGD FVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQ IYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIM HGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQP QNGRSVSKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKA EGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRP QFHQFTAVPHPNVKPMAYANTLLQLGM Description Functional site 1) chain A residue 242 type sequence D description BINDING SITE FOR RESIDUE MG A 501 source : AC1 2) chain A residue 244 type sequence H description BINDING SITE FOR RESIDUE MG A 501 source : AC1 3) chain A residue 271 type sequence D description BINDING SITE FOR RESIDUE MG A 501 source : AC1 4) chain A residue 427 type sequence H description BINDING SITE FOR RESIDUE MG A 501 source : AC1 5) chain A residue 242 type sequence D description BINDING SITE FOR RESIDUE MG A 502 source : AC2 6) chain A residue 271 type sequence D description BINDING SITE FOR RESIDUE MG A 502 source : AC2 7) chain A residue 303 type sequence N description BINDING SITE FOR RESIDUE MG A 502 source : AC2 8) chain A residue 352 type sequence H description BINDING SITE FOR RESIDUE MG A 502 source : AC2 9) chain A residue 427 type sequence H description BINDING SITE FOR RESIDUE MG A 502 source : AC2 10) chain A residue 300-305 type prosite sequence LRGNHE description SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE source prosite : PS00125 11) chain A residue 242 type BINDING sequence D description BINDING => ECO:0000269|PubMed:26182372, ECO:0007744|PDB:4JA7 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 244 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P53041 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 275 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P53041 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 400 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P53041 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 427 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P53041 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 271 type BINDING sequence D description BINDING => ECO:0000269|PubMed:26182372, ECO:0007744|PDB:4JA7, ECO:0007744|PDB:4JA9 source Swiss-Prot : SWS_FT_FI4 17) chain A residue 303 type BINDING sequence N description BINDING => ECO:0000269|PubMed:26182372, ECO:0007744|PDB:4JA7, ECO:0007744|PDB:4JA9 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 352 type BINDING sequence H description BINDING => ECO:0000269|PubMed:26182372, ECO:0007744|PDB:4JA7, ECO:0007744|PDB:4JA9 source Swiss-Prot : SWS_FT_FI4 19) chain A residue 304 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000250|UniProtKB:P53041 source Swiss-Prot : SWS_FT_FI1

Display surface Download Links