eF-site ID 1wao-2 PDB Code 1wao Chain 2 click to enlarge Title PP5 structure Classification HYDROLASE Compound SERINE/THREONINE PROTEIN PHOSPHATASE 5 Source Homo sapiens (Human) (PPP5_HUMAN) Sequence 2:  GALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNA IYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRR AASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKI VKQKAFERAKRSVVDSLDIESMTIEDEYSGPKLEDGKVTI SFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVE TTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIF NGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDN MNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKV LIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSD PQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHE VKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSD LRPQFHQFTAVPHPNVKPMAYANTLLQLG Description Functional site 1) chain 2 residue 242 type sequence D description BINDING SITE FOR RESIDUE MN 2 601 source : AC3 2) chain 2 residue 271 type sequence D description BINDING SITE FOR RESIDUE MN 2 601 source : AC3 3) chain 2 residue 303 type sequence N description BINDING SITE FOR RESIDUE MN 2 601 source : AC3 4) chain 2 residue 352 type sequence H description BINDING SITE FOR RESIDUE MN 2 601 source : AC3 5) chain 2 residue 427 type sequence H description BINDING SITE FOR RESIDUE MN 2 601 source : AC3 6) chain 2 residue 242 type sequence D description BINDING SITE FOR RESIDUE MN 2 602 source : AC4 7) chain 2 residue 244 type sequence H description BINDING SITE FOR RESIDUE MN 2 602 source : AC4 8) chain 2 residue 271 type sequence D description BINDING SITE FOR RESIDUE MN 2 602 source : AC4 9) chain 2 residue 242 type catalytic sequence D description 472 source MCSA : MCSA2 10) chain 2 residue 427 type catalytic sequence H description 472 source MCSA : MCSA2 11) chain 2 residue 244 type catalytic sequence H description 472 source MCSA : MCSA2 12) chain 2 residue 271 type catalytic sequence D description 472 source MCSA : MCSA2 13) chain 2 residue 274 type catalytic sequence D description 472 source MCSA : MCSA2 14) chain 2 residue 275 type catalytic sequence R description 472 source MCSA : MCSA2 15) chain 2 residue 303 type catalytic sequence N description 472 source MCSA : MCSA2 16) chain 2 residue 304 type catalytic sequence H description 472 source MCSA : MCSA2 17) chain 2 residue 352 type catalytic sequence H description 472 source MCSA : MCSA2 18) chain 2 residue 400 type catalytic sequence R description 472 source MCSA : MCSA2 19) chain 2 residue 304 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI1 20) chain 2 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 21) chain 2 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 22) chain 2 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 23) chain 2 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 24) chain 2 residue 244 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 25) chain 2 residue 275 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 26) chain 2 residue 400 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3 27) chain 2 residue 427 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15155720 source Swiss-Prot : SWS_FT_FI3

Display surface Download Links