eF-site ID 1yxu-ABCD PDB Code 1yxu Chain A, B, C, D click to enlarge Title Crystal Structure of Kinase Pim1 in Complex with AMP Classification TRANSFERASE Compound Proto-oncogene serine/threonine-protein kinase Pim-1 Source Homo sapiens (Human) (PIM1_HUMAN) Sequence A:  PLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKD RISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFER PDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVL EAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGAL LKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILL YDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLA LRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLH B:  PLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKD RISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFER PDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVL EAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGAL LKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILL YDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLA LRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLH C:  LESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDR ISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERP DSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLE AVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALL KDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLY DMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLAL RPSDRPTFEEIQNHPWMQDVLLPQETAEIHLH D:  PLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKD RISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFER PDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVL EAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGAL LKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILL YDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLA LRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLH Description Functional site 1) chain A residue 130 type sequence F description BINDING SITE FOR RESIDUE IMD A 500 source : AC1 2) chain A residue 134 type sequence T description BINDING SITE FOR RESIDUE IMD A 500 source : AC1 3) chain A residue 170 type sequence D description BINDING SITE FOR RESIDUE IMD A 500 source : AC1 4) chain A residue 234 type sequence D description BINDING SITE FOR RESIDUE IMD A 500 source : AC1 5) chain A residue 238 type sequence G description BINDING SITE FOR RESIDUE IMD A 500 source : AC1 6) chain A residue 239 type sequence D description BINDING SITE FOR RESIDUE IMD A 500 source : AC1 7) chain B residue 130 type sequence F description BINDING SITE FOR RESIDUE IMD B 600 source : AC2 8) chain B residue 133 type sequence I description BINDING SITE FOR RESIDUE IMD B 600 source : AC2 9) chain B residue 134 type sequence T description BINDING SITE FOR RESIDUE IMD B 600 source : AC2 10) chain B residue 170 type sequence D description BINDING SITE FOR RESIDUE IMD B 600 source : AC2 11) chain B residue 234 type sequence D description BINDING SITE FOR RESIDUE IMD B 600 source : AC2 12) chain B residue 238 type sequence G description BINDING SITE FOR RESIDUE IMD B 600 source : AC2 13) chain B residue 239 type sequence D description BINDING SITE FOR RESIDUE IMD B 600 source : AC2 14) chain C residue 130 type sequence F description BINDING SITE FOR RESIDUE IMD C 700 source : AC3 15) chain C residue 134 type sequence T description BINDING SITE FOR RESIDUE IMD C 700 source : AC3 16) chain C residue 170 type sequence D description BINDING SITE FOR RESIDUE IMD C 700 source : AC3 17) chain C residue 234 type sequence D description BINDING SITE FOR RESIDUE IMD C 700 source : AC3 18) chain C residue 238 type sequence G description BINDING SITE FOR RESIDUE IMD C 700 source : AC3 19) chain D residue 130 type sequence F description BINDING SITE FOR RESIDUE IMD D 800 source : AC4 20) chain D residue 133 type sequence I description BINDING SITE FOR RESIDUE IMD D 800 source : AC4 21) chain D residue 134 type sequence T description BINDING SITE FOR RESIDUE IMD D 800 source : AC4 22) chain D residue 170 type sequence D description BINDING SITE FOR RESIDUE IMD D 800 source : AC4 23) chain D residue 234 type sequence D description BINDING SITE FOR RESIDUE IMD D 800 source : AC4 24) chain D residue 238 type sequence G description BINDING SITE FOR RESIDUE IMD D 800 source : AC4 25) chain D residue 239 type sequence D description BINDING SITE FOR RESIDUE IMD D 800 source : AC4 26) chain A residue 44 type sequence L description BINDING SITE FOR RESIDUE AMP A 550 source : AC5 27) chain A residue 49 type sequence F description BINDING SITE FOR RESIDUE AMP A 550 source : AC5 28) chain A residue 65 type sequence A description BINDING SITE FOR RESIDUE AMP A 550 source : AC5 29) chain A residue 67 type sequence K description BINDING SITE FOR RESIDUE AMP A 550 source : AC5 30) chain A residue 89 type sequence E description BINDING SITE FOR RESIDUE AMP A 550 source : AC5 31) chain A residue 104 type sequence I description BINDING SITE FOR RESIDUE AMP A 550 source : AC5 32) chain A residue 120 type sequence L description BINDING SITE FOR RESIDUE AMP A 550 source : AC5 33) chain A residue 171 type sequence E description BINDING SITE FOR RESIDUE AMP A 550 source : AC5 34) chain A residue 172 type sequence N description BINDING SITE FOR RESIDUE AMP A 550 source : AC5 35) chain A residue 174 type sequence L description BINDING SITE FOR RESIDUE AMP A 550 source : AC5 36) chain A residue 185 type sequence I description BINDING SITE FOR RESIDUE AMP A 550 source : AC5 37) chain A residue 186 type sequence D description BINDING SITE FOR RESIDUE AMP A 550 source : AC5 38) chain B residue 44 type sequence L description BINDING SITE FOR RESIDUE AMP B 650 source : AC6 39) chain B residue 49 type sequence F description BINDING SITE FOR RESIDUE AMP B 650 source : AC6 40) chain B residue 52 type sequence V description BINDING SITE FOR RESIDUE AMP B 650 source : AC6 41) chain B residue 65 type sequence A description BINDING SITE FOR RESIDUE AMP B 650 source : AC6 42) chain B residue 67 type sequence K description BINDING SITE FOR RESIDUE AMP B 650 source : AC6 43) chain B residue 104 type sequence I description BINDING SITE FOR RESIDUE AMP B 650 source : AC6 44) chain B residue 120 type sequence L description BINDING SITE FOR RESIDUE AMP B 650 source : AC6 45) chain B residue 126 type sequence V description BINDING SITE FOR RESIDUE AMP B 650 source : AC6 46) chain B residue 171 type sequence E description BINDING SITE FOR RESIDUE AMP B 650 source : AC6 47) chain B residue 172 type sequence N description BINDING SITE FOR RESIDUE AMP B 650 source : AC6 48) chain B residue 185 type sequence I description BINDING SITE FOR RESIDUE AMP B 650 source : AC6 49) chain B residue 186 type sequence D description BINDING SITE FOR RESIDUE AMP B 650 source : AC6 50) chain C residue 44 type sequence L description BINDING SITE FOR RESIDUE AMP C 750 source : AC7 51) chain C residue 49 type sequence F description BINDING SITE FOR RESIDUE AMP C 750 source : AC7 52) chain C residue 65 type sequence A description BINDING SITE FOR RESIDUE AMP C 750 source : AC7 53) chain C residue 67 type sequence K description BINDING SITE FOR RESIDUE AMP C 750 source : AC7 54) chain C residue 104 type sequence I description BINDING SITE FOR RESIDUE AMP C 750 source : AC7 55) chain C residue 120 type sequence L description BINDING SITE FOR RESIDUE AMP C 750 source : AC7 56) chain C residue 122 type sequence R description BINDING SITE FOR RESIDUE AMP C 750 source : AC7 57) chain C residue 126 type sequence V description BINDING SITE FOR RESIDUE AMP C 750 source : AC7 58) chain C residue 171 type sequence E description BINDING SITE FOR RESIDUE AMP C 750 source : AC7 59) chain C residue 172 type sequence N description BINDING SITE FOR RESIDUE AMP C 750 source : AC7 60) chain C residue 174 type sequence L description BINDING SITE FOR RESIDUE AMP C 750 source : AC7 61) chain C residue 185 type sequence I description BINDING SITE FOR RESIDUE AMP C 750 source : AC7 62) chain C residue 186 type sequence D description BINDING SITE FOR RESIDUE AMP C 750 source : AC7 63) chain D residue 49 type sequence F description BINDING SITE FOR RESIDUE AMP D 850 source : AC8 64) chain D residue 52 type sequence V description BINDING SITE FOR RESIDUE AMP D 850 source : AC8 65) chain D residue 65 type sequence A description BINDING SITE FOR RESIDUE AMP D 850 source : AC8 66) chain D residue 67 type sequence K description BINDING SITE FOR RESIDUE AMP D 850 source : AC8 67) chain D residue 89 type sequence E description BINDING SITE FOR RESIDUE AMP D 850 source : AC8 68) chain D residue 104 type sequence I description BINDING SITE FOR RESIDUE AMP D 850 source : AC8 69) chain D residue 120 type sequence L description BINDING SITE FOR RESIDUE AMP D 850 source : AC8 70) chain D residue 121 type sequence E description BINDING SITE FOR RESIDUE AMP D 850 source : AC8 71) chain D residue 122 type sequence R description BINDING SITE FOR RESIDUE AMP D 850 source : AC8 72) chain D residue 174 type sequence L description BINDING SITE FOR RESIDUE AMP D 850 source : AC8 73) chain D residue 185 type sequence I description BINDING SITE FOR RESIDUE AMP D 850 source : AC8 74) chain D residue 186 type sequence D description BINDING SITE FOR RESIDUE AMP D 850 source : AC8 75) chain A residue 167 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 76) chain B residue 167 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 77) chain C residue 167 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 78) chain D residue 167 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 79) chain A residue 44-67 type prosite sequence LGSGGFGSVYSGIRVSDNLPVAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGGFGSVYsGirvsdnlp..........VAIK source prosite : PS00107 80) chain A residue 163-175 type prosite sequence VLHRDIKDENILI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI source prosite : PS00108 81) chain A residue 44 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 82) chain B residue 44 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 83) chain C residue 44 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 84) chain D residue 44 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 85) chain A residue 98 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI4 86) chain A residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI4 87) chain B residue 98 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI4 88) chain B residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI4 89) chain C residue 98 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI4 90) chain C residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI4 91) chain D residue 98 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI4 92) chain D residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI4 93) chain A residue 67 type BINDING sequence K description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 94) chain D residue 67 type BINDING sequence K description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 95) chain D residue 121 type BINDING sequence E description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 96) chain D residue 128 type BINDING sequence D description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 97) chain A residue 121 type BINDING sequence E description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 98) chain A residue 128 type BINDING sequence D description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 99) chain B residue 67 type BINDING sequence K description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 100) chain B residue 121 type BINDING sequence E description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 101) chain B residue 128 type BINDING sequence D description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 102) chain C residue 67 type BINDING sequence K description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 103) chain C residue 121 type BINDING sequence E description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 104) chain C residue 128 type BINDING sequence D description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3

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