eF-site ID 1s95-A PDB Code 1s95 Chain A click to enlarge Title Structure of serine/threonine protein phosphatase 5 Classification HYDROLASE Compound Serine/threonine protein phosphatase 5 Source Homo sapiens (Human) (PPP5_HUMAN) Sequence A:  YSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQ VKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFE LNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPD HFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVF EWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQP PDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFL EENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQM GNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYANTLLQ LGMM Description Functional site 1) chain A residue 242 type sequence D description BINDING SITE FOR RESIDUE MN A 501 source : AC1 2) chain A residue 244 type sequence H description BINDING SITE FOR RESIDUE MN A 501 source : AC1 3) chain A residue 271 type sequence D description BINDING SITE FOR RESIDUE MN A 501 source : AC1 4) chain A residue 271 type sequence D description BINDING SITE FOR RESIDUE MN A 502 source : AC2 5) chain A residue 303 type sequence N description BINDING SITE FOR RESIDUE MN A 502 source : AC2 6) chain A residue 352 type sequence H description BINDING SITE FOR RESIDUE MN A 502 source : AC2 7) chain A residue 427 type sequence H description BINDING SITE FOR RESIDUE MN A 502 source : AC2 8) chain A residue 244 type sequence H description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 9) chain A residue 271 type sequence D description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 10) chain A residue 275 type sequence R description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 11) chain A residue 303 type sequence N description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 12) chain A residue 304 type sequence H description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 13) chain A residue 400 type sequence R description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 14) chain A residue 427 type sequence H description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 15) chain A residue 192 type sequence K description BINDING SITE FOR RESIDUE MPD A 3001 source : AC7 16) chain A residue 251 type sequence L description BINDING SITE FOR RESIDUE MPD A 3001 source : AC7 17) chain A residue 255 type sequence E description BINDING SITE FOR RESIDUE MPD A 3001 source : AC7 18) chain A residue 242 type catalytic sequence D description 472 source MCSA : MCSA1 19) chain A residue 427 type catalytic sequence H description 472 source MCSA : MCSA1 20) chain A residue 244 type catalytic sequence H description 472 source MCSA : MCSA1 21) chain A residue 271 type catalytic sequence D description 472 source MCSA : MCSA1 22) chain A residue 274 type catalytic sequence D description 472 source MCSA : MCSA1 23) chain A residue 275 type catalytic sequence R description 472 source MCSA : MCSA1 24) chain A residue 303 type catalytic sequence N description 472 source MCSA : MCSA1 25) chain A residue 304 type catalytic sequence H description 472 source MCSA : MCSA1 26) chain A residue 352 type catalytic sequence H description 472 source MCSA : MCSA1 27) chain A residue 400 type catalytic sequence R description 472 source MCSA : MCSA1 28) chain A residue 244 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 275 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 400 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 427 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 242 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15155720, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:19601647, ECO:0007744|PDB:1S95, ECO:0007744|PDB:1WAO, ECO:0007744|PDB:3H60, ECO:0007744|PDB:3H61, ECO:0007744|PDB:3H62, ECO:0007744|PDB:3H63, ECO:0007744|PDB:3H64 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 271 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15155720, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:19601647, ECO:0007744|PDB:1S95, ECO:0007744|PDB:1WAO, ECO:0007744|PDB:3H60, ECO:0007744|PDB:3H61, ECO:0007744|PDB:3H62, ECO:0007744|PDB:3H63, ECO:0007744|PDB:3H64 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 303 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15155720, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:19601647, ECO:0007744|PDB:1S95, ECO:0007744|PDB:1WAO, ECO:0007744|PDB:3H60, ECO:0007744|PDB:3H61, ECO:0007744|PDB:3H62, ECO:0007744|PDB:3H63, ECO:0007744|PDB:3H64 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 352 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15155720, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:19601647, ECO:0007744|PDB:1S95, ECO:0007744|PDB:1WAO, ECO:0007744|PDB:3H60, ECO:0007744|PDB:3H61, ECO:0007744|PDB:3H62, ECO:0007744|PDB:3H63, ECO:0007744|PDB:3H64 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 304 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 300-305 type prosite sequence LRGNHE description SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE source prosite : PS00125

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