eF-site ID 1s95-AB PDB Code 1s95 Chain A, B click to enlarge Title Structure of serine/threonine protein phosphatase 5 Classification HYDROLASE Compound Serine/threonine protein phosphatase 5 Source null (PPP5_HUMAN) Sequence A:  YSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQ VKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFE LNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPD HFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVF EWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQP PDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFL EENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQM GNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYANTLLQ LGMM B:  EYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILV QVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIF ELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYP DHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEV FEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQ PPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAF LEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQ MGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYANTLL QLGMM 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 B residue 242 type sequence D description BINDING SITE FOR RESIDUE MN B 601 source : AC3 9) chain B residue 244 type sequence H description BINDING SITE FOR RESIDUE MN B 601 source : AC3 10) chain B residue 271 type sequence D description BINDING SITE FOR RESIDUE MN B 601 source : AC3 11) chain B residue 271 type sequence D description BINDING SITE FOR RESIDUE MN B 602 source : AC4 12) chain B residue 303 type sequence N description BINDING SITE FOR RESIDUE MN B 602 source : AC4 13) chain B residue 352 type sequence H description BINDING SITE FOR RESIDUE MN B 602 source : AC4 14) chain B residue 427 type sequence H description BINDING SITE FOR RESIDUE MN B 602 source : AC4 15) chain A residue 244 type sequence H description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 16) chain A residue 271 type sequence D description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 17) chain A residue 275 type sequence R description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 18) chain A residue 303 type sequence N description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 19) chain A residue 304 type sequence H description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 20) chain A residue 400 type sequence R description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 21) chain A residue 427 type sequence H description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 22) chain B residue 499 type sequence M description BINDING SITE FOR RESIDUE PO4 A 1001 source : AC5 23) chain B residue 244 type sequence H description BINDING SITE FOR RESIDUE PO4 B 2001 source : AC6 24) chain B residue 271 type sequence D description BINDING SITE FOR RESIDUE PO4 B 2001 source : AC6 25) chain B residue 275 type sequence R description BINDING SITE FOR RESIDUE PO4 B 2001 source : AC6 26) chain B residue 303 type sequence N description BINDING SITE FOR RESIDUE PO4 B 2001 source : AC6 27) chain B residue 304 type sequence H description BINDING SITE FOR RESIDUE PO4 B 2001 source : AC6 28) chain B residue 400 type sequence R description BINDING SITE FOR RESIDUE PO4 B 2001 source : AC6 29) chain B residue 427 type sequence H description BINDING SITE FOR RESIDUE PO4 B 2001 source : AC6 30) chain A residue 192 type sequence K description BINDING SITE FOR RESIDUE MPD A 3001 source : AC7 31) chain A residue 251 type sequence L description BINDING SITE FOR RESIDUE MPD A 3001 source : AC7 32) chain A residue 255 type sequence E description BINDING SITE FOR RESIDUE MPD A 3001 source : AC7 33) chain B residue 192 type sequence K description BINDING SITE FOR RESIDUE MPD B 3002 source : AC8 34) chain B residue 196 type sequence Q description BINDING SITE FOR RESIDUE MPD B 3002 source : AC8 35) chain B residue 255 type sequence E description BINDING SITE FOR RESIDUE MPD B 3002 source : AC8 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 B residue 304 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI1 38) 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 39) 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 40) 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 41) 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 42) chain B 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 43) chain B 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 44) chain B 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 45) chain B 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 46) chain A residue 244 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 47) chain A residue 275 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 400 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 427 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 50) chain B residue 244 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 51) chain B residue 275 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 52) chain B residue 400 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 53) chain B residue 427 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 54) chain A residue 242 type catalytic sequence D description 472 source MCSA : MCSA1 55) chain A residue 244 type catalytic sequence H description 472 source MCSA : MCSA1 56) chain A residue 271 type catalytic sequence D description 472 source MCSA : MCSA1 57) chain A residue 274 type catalytic sequence D description 472 source MCSA : MCSA1 58) chain A residue 275 type catalytic sequence R description 472 source MCSA : MCSA1 59) chain A residue 303 type catalytic sequence N description 472 source MCSA : MCSA1 60) chain A residue 304 type catalytic sequence H description 472 source MCSA : MCSA1 61) chain A residue 352 type catalytic sequence H description 472 source MCSA : MCSA1 62) chain A residue 400 type catalytic sequence R description 472 source MCSA : MCSA1 63) chain A residue 427 type catalytic sequence H description 472 source MCSA : MCSA1 64) chain B residue 242 type catalytic sequence D description 472 source MCSA : MCSA2 65) chain B residue 244 type catalytic sequence H description 472 source MCSA : MCSA2 66) chain B residue 271 type catalytic sequence D description 472 source MCSA : MCSA2 67) chain B residue 274 type catalytic sequence D description 472 source MCSA : MCSA2 68) chain B residue 275 type catalytic sequence R description 472 source MCSA : MCSA2 69) chain B residue 303 type catalytic sequence N description 472 source MCSA : MCSA2 70) chain B residue 304 type catalytic sequence H description 472 source MCSA : MCSA2 71) chain B residue 352 type catalytic sequence H description 472 source MCSA : MCSA2 72) chain B residue 400 type catalytic sequence R description 472 source MCSA : MCSA2 73) chain B residue 427 type catalytic sequence H description 472 source MCSA : MCSA2 74) chain A residue 300-305 type prosite sequence LRGNHE description SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE source prosite : PS00125

Display surface Download Links