eF-site ID 5zqv-ABCDEFGH PDB Code 5zqv Chain A, B, C, D, E, F, G, H click to enlarge Title Crystal Structure of Protein Phosphate 1 complexed with PP1 binding domain of GM Classification HYDROLASE Compound Serine/threonine-protein phosphatase PP1-alpha catalytic subunit Source (PPR3A_HUMAN) Sequence A:  KLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREI FLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPES NYLFLGDYVDRGKQSLETICLLLAYKIRYPENFFLLRGNH ECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIV DEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLL WSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLIC RAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSV DETLMCSFQILKPA B:  LNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIF LSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESN YLFLGDYVDRGKQSLETICLLLAYKIRYPENFFLLRGNHE CASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVD EKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLW SDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICR AHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVD ETLMCSFQILKPA C:  KLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREI FLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPES NYLFLGDYVDRGKQSLETICLLLAYKIRYPENFFLLRGNH ECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIV DEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLL WSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLIC RAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSV DETLMCSFQILKPA D:  KLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREI FLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPES NYLFLGDYVDRGKQSLETICLLLAYKIRYPENFFLLRGNH ECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIV DEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLL WSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLIC RAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSV DETLMCSFQILKPA E:  TRRVSFADSFGFNLVSVKEFD F:  TRRVSFADSFGFNLVSVKEFD G:  RRVSFADSFGFNLVSVKEFD H:  TRRVSFADSFGFNLVSVKEFD Description Functional site 1) chain A residue 92 type sequence D description binding site for residue MN A 401 source : AC1 2) chain A residue 124 type sequence N description binding site for residue MN A 401 source : AC1 3) chain A residue 173 type sequence H description binding site for residue MN A 401 source : AC1 4) chain A residue 248 type sequence H description binding site for residue MN A 401 source : AC1 5) chain A residue 96 type sequence R description binding site for residue FLC A 402 source : AC2 6) chain A residue 124 type sequence N description binding site for residue FLC A 402 source : AC2 7) chain A residue 125 type sequence H description binding site for residue FLC A 402 source : AC2 8) chain A residue 134 type sequence Y description binding site for residue FLC A 402 source : AC2 9) chain A residue 221 type sequence R description binding site for residue FLC A 402 source : AC2 10) chain A residue 248 type sequence H description binding site for residue FLC A 402 source : AC2 11) chain C residue 132 type sequence R description binding site for residue FLC A 402 source : AC2 12) chain B residue 92 type sequence D description binding site for residue MN B 401 source : AC3 13) chain B residue 124 type sequence N description binding site for residue MN B 401 source : AC3 14) chain B residue 173 type sequence H description binding site for residue MN B 401 source : AC3 15) chain B residue 248 type sequence H description binding site for residue MN B 401 source : AC3 16) chain C residue 92 type sequence D description binding site for residue MN C 401 source : AC4 17) chain C residue 124 type sequence N description binding site for residue MN C 401 source : AC4 18) chain C residue 173 type sequence H description binding site for residue MN C 401 source : AC4 19) chain C residue 248 type sequence H description binding site for residue MN C 401 source : AC4 20) chain A residue 132 type sequence R description binding site for residue FLC C 402 source : AC5 21) chain A residue 133 type sequence I description binding site for residue FLC C 402 source : AC5 22) chain C residue 124 type sequence N description binding site for residue FLC C 402 source : AC5 23) chain C residue 125 type sequence H description binding site for residue FLC C 402 source : AC5 24) chain C residue 134 type sequence Y description binding site for residue FLC C 402 source : AC5 25) chain C residue 206 type sequence W description binding site for residue FLC C 402 source : AC5 26) chain C residue 221 type sequence R description binding site for residue FLC C 402 source : AC5 27) chain D residue 92 type sequence D description binding site for residue MN D 401 source : AC6 28) chain D residue 124 type sequence N description binding site for residue MN D 401 source : AC6 29) chain D residue 173 type sequence H description binding site for residue MN D 401 source : AC6 30) chain D residue 248 type sequence H description binding site for residue MN D 401 source : AC6 31) chain B residue 132 type sequence R description binding site for residue FLC D 402 source : AC7 32) chain D residue 96 type sequence R description binding site for residue FLC D 402 source : AC7 33) chain D residue 124 type sequence N description binding site for residue FLC D 402 source : AC7 34) chain D residue 125 type sequence H description binding site for residue FLC D 402 source : AC7 35) chain D residue 134 type sequence Y description binding site for residue FLC D 402 source : AC7 36) chain D residue 206 type sequence W description binding site for residue FLC D 402 source : AC7 37) chain D residue 221 type sequence R description binding site for residue FLC D 402 source : AC7 38) chain D residue 248 type sequence H description binding site for residue FLC D 402 source : AC7 39) chain B residue 124 type MOD_RES sequence N description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 173 type MOD_RES sequence H description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 41) chain B residue 248 type MOD_RES sequence H description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 42) chain C residue 64 type MOD_RES sequence D description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 43) chain C residue 66 type MOD_RES sequence H description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 44) chain C residue 92 type MOD_RES sequence D description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 45) chain C residue 124 type MOD_RES sequence N description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 46) chain C residue 173 type MOD_RES sequence H description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 47) chain C residue 248 type MOD_RES sequence H description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 48) chain D residue 64 type MOD_RES sequence D description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 49) chain D residue 66 type MOD_RES sequence H description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 50) chain D residue 92 type MOD_RES sequence D description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 51) chain D residue 124 type MOD_RES sequence N description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 52) chain D residue 173 type MOD_RES sequence H description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 53) chain D residue 248 type MOD_RES sequence H description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 173 type MOD_RES sequence H description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 248 type MOD_RES sequence H description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 56) chain B residue 64 type MOD_RES sequence D description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 57) chain B residue 66 type MOD_RES sequence H description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 58) chain B residue 92 type MOD_RES sequence D description Phosphoserine; by PKA and ISPK => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI2 59) chain D residue 22 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q99MR9 source Swiss-Prot : SWS_FT_FI3 60) chain B residue 22 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q99MR9 source Swiss-Prot : SWS_FT_FI3 61) chain C residue 22 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q99MR9 source Swiss-Prot : SWS_FT_FI3 62) chain A residue 121-126 type prosite sequence LRGNHE description SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE source prosite : PS00125 63) chain E residue 65 type MOD_RES sequence S description Phosphoserine; by PKA => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI5 64) chain F residue 65 type MOD_RES sequence S description Phosphoserine; by PKA => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI5 65) chain G residue 65 type MOD_RES sequence S description Phosphoserine; by PKA => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI5 66) chain H residue 65 type MOD_RES sequence S description Phosphoserine; by PKA => ECO:0000250|UniProtKB:Q00756 source Swiss-Prot : SWS_FT_FI5

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