eF-site ID 1qol-ABCDEFGH PDB Code 1qol Chain A, B, C, D, E, F, G, H click to enlarge Title STRUCTURE OF THE FMDV LEADER PROTEASE Classification HYDROLASE Compound PROTEASE (NONSTRUCTURAL PROTEIN P20A) Source (POLG_FMDVO) Sequence A:  MELTLYNGEKKTFYSRPNNHDNAWLNAILQLFRYVEEPFF DWVYSSPENLTLEAIKQLEDLTGLELHEGGPPALVIWNIK HLLHTGIGTASRPSEVCVVDGTDMCLADFHAGIFLKGQEH AVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQKAK VQRKLK B:  MELTLYNGEKKTFYSRPNNHDNAWLNAILQLFRYVEEPFF DWVYSSPENLTLEAIKQLEDLTGLELHEGGPPALVIWNIK HLLHTGIGTASRPSEVCVVDGTDMCLADFHAGIFLKGQEH AVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQKAK VQRKLK C:  MELTLYNGEKKTFYSRPNNHDNAWLNAILQLFRYVEEPFF DWVYSSPENLTLEAIKQLEDLTGLELHEGGPPALVIWNIK HLLHTGIGTASRPSEVCVVDGTDMCLADFHAGIFLKGQEH AVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQEPL NGEWKAKVQRKLK D:  MELTLYNGEKKTFYSRPNNHDNAWLNAILQLFRYVEEPFF DWVYSSPENLTLEAIKQLEDLTGLELHEGGPPALVIWNIK HLLHTGIGTASRPSEVCVVDGTDMCLADFHAGIFLKGQEH AVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQEPL NGEWKAKVQRKLK E:  MELTLYNGEKKTFYSRPNNHDNAWLNAILQLFRYVEEPFF DWVYSSPENLTLEAIKQLEDLTGLELHEGGPPALVIWNIK HLLHTGIGTASRPSEVCVVDGTDMCLADFHAGIFLKGQEH AVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQKAK VQRKLK F:  MELTLYNGEKKTFYSRPNNHDNAWLNAILQLFRYVEEPFF DWVYSSPENLTLEAIKQLEDLTGLELHEGGPPALVIWNIK HLLHTGIGTASRPSEVCVVDGTDMCLADFHAGIFLKGQEH AVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQKAK VQRKLK G:  MELTLYNGEKKTFYSRPNNHDNAWLNAILQLFRYVEEPFF DWVYSSPENLTLEAIKQLEDLTGLELHEGGPPALVIWNIK HLLHTGIGTASRPSEVCVVDGTDMCLADFHAGIFLKGQEH AVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQEPL NGEWKAKVQRKLK H:  MELTLYNGEKKTFYSRPNNHDNAWLNAILQLFRYVEEPFF DWVYSSPENLTLEAIKQLEDLTGLELHEGGPPALVIWNIK HLLHTGIGTASRPSEVCVVDGTDMCLADFHAGIFLKGQEH AVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQEPL NGEWKAKVQRKLK Description (1)  PROTEASE (NONSTRUCTURAL PROTEIN P20A) Functional site 1) chain A residue 135 type sequence A description BINDING SITE FOR RESIDUE CL Z 1 source : AC1 2) chain D residue 134 type sequence L description BINDING SITE FOR RESIDUE CL Z 1 source : AC1 3) chain D residue 135 type sequence A description BINDING SITE FOR RESIDUE CL Z 1 source : AC1 4) chain B residue 135 type sequence A description BINDING SITE FOR RESIDUE CL Z 2 source : AC2 5) chain C residue 135 type sequence A description BINDING SITE FOR RESIDUE CL Z 2 source : AC2 6) chain E residue 133 type sequence C description BINDING SITE FOR RESIDUE CL Z 3 source : AC3 7) chain E residue 135 type sequence A description BINDING SITE FOR RESIDUE CL Z 3 source : AC3 8) chain G residue 133 type sequence C description BINDING SITE FOR RESIDUE CL Z 3 source : AC3 9) chain G residue 134 type sequence L description BINDING SITE FOR RESIDUE CL Z 3 source : AC3 10) chain G residue 135 type sequence A description BINDING SITE FOR RESIDUE CL Z 3 source : AC3 11) chain A residue 76 type sequence E description BINDING SITE FOR RESIDUE EDO A 301 source : AC4 12) chain A residue 77 type sequence N description BINDING SITE FOR RESIDUE EDO A 301 source : AC4 13) chain A residue 81 type sequence E description BINDING SITE FOR RESIDUE EDO A 301 source : AC4 14) chain F residue 76 type sequence E description BINDING SITE FOR RESIDUE EDO A 301 source : AC4 15) chain B residue 77 type sequence N description BINDING SITE FOR RESIDUE EDO B 301 source : AC5 16) chain B residue 81 type sequence E description BINDING SITE FOR RESIDUE EDO B 301 source : AC5 17) chain E residue 76 type sequence E description BINDING SITE FOR RESIDUE EDO B 301 source : AC5 18) chain A residue 46 type catalytic sequence N description 746 source MCSA : MCSA1 19) chain A residue 51 type catalytic sequence A description 746 source MCSA : MCSA1 20) chain A residue 148 type catalytic sequence H description 746 source MCSA : MCSA1 21) chain A residue 163 type catalytic sequence D description 746 source MCSA : MCSA1 22) chain B residue 46 type catalytic sequence N description 746 source MCSA : MCSA2 23) chain B residue 51 type catalytic sequence A description 746 source MCSA : MCSA2 24) chain B residue 148 type catalytic sequence H description 746 source MCSA : MCSA2 25) chain B residue 163 type catalytic sequence D description 746 source MCSA : MCSA2 26) chain C residue 46 type catalytic sequence N description 746 source MCSA : MCSA3 27) chain C residue 51 type catalytic sequence A description 746 source MCSA : MCSA3 28) chain C residue 148 type catalytic sequence H description 746 source MCSA : MCSA3 29) chain C residue 163 type catalytic sequence D description 746 source MCSA : MCSA3 30) chain D residue 46 type catalytic sequence N description 746 source MCSA : MCSA4 31) chain D residue 51 type catalytic sequence A description 746 source MCSA : MCSA4 32) chain D residue 148 type catalytic sequence H description 746 source MCSA : MCSA4 33) chain D residue 163 type catalytic sequence D description 746 source MCSA : MCSA4 34) chain E residue 46 type catalytic sequence N description 746 source MCSA : MCSA5 35) chain E residue 51 type catalytic sequence A description 746 source MCSA : MCSA5 36) chain E residue 148 type catalytic sequence H description 746 source MCSA : MCSA5 37) chain E residue 163 type catalytic sequence D description 746 source MCSA : MCSA5 38) chain F residue 46 type catalytic sequence N description 746 source MCSA : MCSA6 39) chain F residue 51 type catalytic sequence A description 746 source MCSA : MCSA6 40) chain F residue 148 type catalytic sequence H description 746 source MCSA : MCSA6 41) chain F residue 163 type catalytic sequence D description 746 source MCSA : MCSA6 42) chain G residue 46 type catalytic sequence N description 746 source MCSA : MCSA7 43) chain G residue 51 type catalytic sequence A description 746 source MCSA : MCSA7 44) chain G residue 148 type catalytic sequence H description 746 source MCSA : MCSA7 45) chain G residue 163 type catalytic sequence D description 746 source MCSA : MCSA7 46) chain H residue 46 type catalytic sequence N description 746 source MCSA : MCSA8 47) chain H residue 51 type catalytic sequence A description 746 source MCSA : MCSA8 48) chain H residue 148 type catalytic sequence H description 746 source MCSA : MCSA8 49) chain H residue 163 type catalytic sequence D description 746 source MCSA : MCSA8 50) chain A residue 51 type ACT_SITE sequence A description For leader protease activity source Swiss-Prot : SWS_FT_FI1 51) chain D residue 51 type ACT_SITE sequence A description For leader protease activity source Swiss-Prot : SWS_FT_FI1 52) chain D residue 148 type ACT_SITE sequence H description For leader protease activity source Swiss-Prot : SWS_FT_FI1 53) chain D residue 163 type ACT_SITE sequence D description For leader protease activity source Swiss-Prot : SWS_FT_FI1 54) chain E residue 51 type ACT_SITE sequence A description For leader protease activity source Swiss-Prot : SWS_FT_FI1 55) chain E residue 148 type ACT_SITE sequence H description For leader protease activity source Swiss-Prot : SWS_FT_FI1 56) chain E residue 163 type ACT_SITE sequence D description For leader protease activity source Swiss-Prot : SWS_FT_FI1 57) chain F residue 51 type ACT_SITE sequence A description For leader protease activity source Swiss-Prot : SWS_FT_FI1 58) chain F residue 148 type ACT_SITE sequence H description For leader protease activity source Swiss-Prot : SWS_FT_FI1 59) chain F residue 163 type ACT_SITE sequence D description For leader protease activity source Swiss-Prot : SWS_FT_FI1 60) chain G residue 51 type ACT_SITE sequence A description For leader protease activity source Swiss-Prot : SWS_FT_FI1 61) chain A residue 148 type ACT_SITE sequence H description For leader protease activity source Swiss-Prot : SWS_FT_FI1 62) chain G residue 148 type ACT_SITE sequence H description For leader protease activity source Swiss-Prot : SWS_FT_FI1 63) chain G residue 163 type ACT_SITE sequence D description For leader protease activity source Swiss-Prot : SWS_FT_FI1 64) chain H residue 51 type ACT_SITE sequence A description For leader protease activity source Swiss-Prot : SWS_FT_FI1 65) chain H residue 148 type ACT_SITE sequence H description For leader protease activity source Swiss-Prot : SWS_FT_FI1 66) chain H residue 163 type ACT_SITE sequence D description For leader protease activity source Swiss-Prot : SWS_FT_FI1 67) chain A residue 163 type ACT_SITE sequence D description For leader protease activity source Swiss-Prot : SWS_FT_FI1 68) chain B residue 51 type ACT_SITE sequence A description For leader protease activity source Swiss-Prot : SWS_FT_FI1 69) chain B residue 148 type ACT_SITE sequence H description For leader protease activity source Swiss-Prot : SWS_FT_FI1 70) chain B residue 163 type ACT_SITE sequence D description For leader protease activity source Swiss-Prot : SWS_FT_FI1 71) chain C residue 51 type ACT_SITE sequence A description For leader protease activity source Swiss-Prot : SWS_FT_FI1 72) chain C residue 148 type ACT_SITE sequence H description For leader protease activity source Swiss-Prot : SWS_FT_FI1 73) chain C residue 163 type ACT_SITE sequence D description For leader protease activity source Swiss-Prot : SWS_FT_FI1 74) chain A residue 201 type SITE sequence K description Cleavage; by leader protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 75) chain B residue 201 type SITE sequence K description Cleavage; by leader protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 76) chain C residue 201 type SITE sequence K description Cleavage; by leader protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 77) chain D residue 201 type SITE sequence K description Cleavage; by leader protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 78) chain E residue 201 type SITE sequence K description Cleavage; by leader protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 79) chain F residue 201 type SITE sequence K description Cleavage; by leader protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 80) chain G residue 201 type SITE sequence K description Cleavage; by leader protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 81) chain H residue 201 type SITE sequence K description Cleavage; by leader protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI2

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