eF-site ID 2ypt-ABDEFGHI PDB Code 2ypt Chain A, B, D, E, F, G, H, I click to enlarge Title Crystal structure of the human nuclear membrane zinc metalloprotease ZMPSTE24 mutant (E336A) in complex with a synthetic CSIM tetrapeptide from the C-terminus of prelamin A Classification HYDROLASE/PEPTIDE Compound CAAX PRENYL PROTEASE 1 HOMOLOG Source Homo sapiens (Human) (LMNA_HUMAN) Sequence A:  GMWASLDALWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQ RRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSFWS GLYSETEGTLILLFGGIPYLWRLSGRPEYEITQSLVFLLL ATLFSALAGLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIK KFVVTQCILLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSL VLVTIYADYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPL TKVYVVEGSKRSSHSNAYFYGFKRIVLFDTLLEQGCKNEE VLAVLGHALGHWKLGHTVKNIIISQMNSFLCFFLFAVLIG RKELFAAFGFYDSQPTLIGLLIIFQFIFSPYNEVLSFCLT VLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVS DWLFSMWHYSHPPLLERLQALKTM B:  LWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTT HVPPELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSETEG TLILLFGGIPYLWRLSGRPEYEITQSLVFLLLATLFSALA GLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIKKFVVTQCI LLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYAD YIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVEG SKRSSHSNAYFYGFKRIVLFDTLLEQGCKNEEVLAVLGHA LGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAF GFYDSQPTLIGLLIIFQFIFSPYNEVLSFCLTVLSRRFEF QADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSMWH YSHPPLLERLQALKTM D:  LWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTT HVPPELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSETEG TLILLFGGIPYLWRLSGRPEYEITQSLVFLLLATLFSALA GLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIKKFVVTQCI LLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYAD YIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVEG SKRSSHSNAYFYGFKRIVLFDTLLEQGCKNEEVLAVLGHA LGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAF GFYDSQPTLIGLLIIFQFIFSPYNEVLSFCLTVLSRRFEF QADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSMWH YSHPPLLERLQALKT E:  LWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTT HVPPELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSETEG TLILLFGGIPYLWRLSGRPEYEITQSLVFLLLATLFSALA GLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIKKFVVTQCI LLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYAD YIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVEG SKRSSHSNAYFYGFKRIVLFDTLLEGCKNEEVLAVLGHAL GHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAFG FYDSQPTLIGLLIIFQFIFSPYNEVLSFCLTVLSRRFEFQ ADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSMWHY SHPPLLERLQALKT F:  CSI G:  CSIM H:  CSIM I:  CSI Description (1)  CAAX PRENYL PROTEASE 1 HOMOLOG (E.C.3.4.24.84), PRELAMIN-A/C Functional site 1) chain A residue 335 type sequence H description BINDING SITE FOR RESIDUE ZN A 600 source : AC1 2) chain A residue 339 type sequence H description BINDING SITE FOR RESIDUE ZN A 600 source : AC1 3) chain A residue 415 type sequence E description BINDING SITE FOR RESIDUE ZN A 600 source : AC1 4) chain F residue 662 type sequence S description BINDING SITE FOR RESIDUE ZN A 600 source : AC1 5) chain B residue 335 type sequence H description BINDING SITE FOR RESIDUE ZN B 600 source : AC2 6) chain B residue 339 type sequence H description BINDING SITE FOR RESIDUE ZN B 600 source : AC2 7) chain B residue 415 type sequence E description BINDING SITE FOR RESIDUE ZN B 600 source : AC2 8) chain G residue 662 type sequence S description BINDING SITE FOR RESIDUE ZN B 600 source : AC2 9) chain D residue 335 type sequence H description BINDING SITE FOR RESIDUE ZN D 600 source : AC3 10) chain D residue 339 type sequence H description BINDING SITE FOR RESIDUE ZN D 600 source : AC3 11) chain D residue 415 type sequence E description BINDING SITE FOR RESIDUE ZN D 600 source : AC3 12) chain H residue 662 type sequence S description BINDING SITE FOR RESIDUE ZN D 600 source : AC3 13) chain E residue 335 type sequence H description BINDING SITE FOR RESIDUE ZN E 600 source : AC4 14) chain E residue 339 type sequence H description BINDING SITE FOR RESIDUE ZN E 600 source : AC4 15) chain E residue 415 type sequence E description BINDING SITE FOR RESIDUE ZN E 600 source : AC4 16) chain I residue 662 type sequence S description BINDING SITE FOR RESIDUE ZN E 600 source : AC4 17) chain F residue 661 type MOD_RES sequence C description Cysteine methyl ester => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI1 18) chain D residue 103-123 type MOD_RES sequence RLSGRPEYEITQS description Cysteine methyl ester => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI1 19) chain D residue 192-195 type MOD_RES sequence GGDY description Cysteine methyl ester => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI1 20) chain D residue 369-382 type MOD_RES sequence RKELFAAFGFYDSQ description Cysteine methyl ester => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI1 21) chain E residue 103-123 type MOD_RES sequence RLSGRPEYEITQS description Cysteine methyl ester => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI1 22) chain E residue 192-195 type MOD_RES sequence GGDY description Cysteine methyl ester => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI1 23) chain E residue 369-382 type MOD_RES sequence RKELFAAFGFYDSQ description Cysteine methyl ester => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI1 24) chain G residue 661 type MOD_RES sequence C description Cysteine methyl ester => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI1 25) chain H residue 661 type MOD_RES sequence C description Cysteine methyl ester => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI1 26) chain I residue 661 type MOD_RES sequence C description Cysteine methyl ester => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 103-123 type MOD_RES sequence RLSGRPEYEITQS description Cysteine methyl ester => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 192-195 type MOD_RES sequence GGDY description Cysteine methyl ester => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 369-382 type MOD_RES sequence RKELFAAFGFYDSQ description Cysteine methyl ester => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI1 30) chain F residue 661 type LIPID sequence C description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 31) chain B residue 124-144 type LIPID sequence LVFLLLATLFSALAGLPWSLY description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 171-191 type LIPID sequence FVVTQCILLPVSSLLLYIIKI description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 196-216 type LIPID sequence FFIYAWLFTLVVSLVLVTIYA description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 34) chain B residue 348-368 type LIPID sequence NIIISQMNSFLCFFLFAVLIG description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 383-405 type LIPID sequence PTLIGLLIIFQFIFSPYNEVLSF description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 36) chain D residue 19-39 type LIPID sequence IFGAVLLFSWTVYLWETFLAQ description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 37) chain D residue 82-102 type LIPID sequence GLYSETEGTLILLFGGIPYLW description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 38) chain D residue 124-144 type LIPID sequence LVFLLLATLFSALAGLPWSLY description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 39) chain D residue 171-191 type LIPID sequence FVVTQCILLPVSSLLLYIIKI description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 40) chain D residue 196-216 type LIPID sequence FFIYAWLFTLVVSLVLVTIYA description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 41) chain G residue 661 type LIPID sequence C description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 42) chain D residue 348-368 type LIPID sequence NIIISQMNSFLCFFLFAVLIG description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 43) chain D residue 383-405 type LIPID sequence PTLIGLLIIFQFIFSPYNEVLSF description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 44) chain E residue 19-39 type LIPID sequence IFGAVLLFSWTVYLWETFLAQ description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 45) chain E residue 82-102 type LIPID sequence GLYSETEGTLILLFGGIPYLW description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 46) chain E residue 124-144 type LIPID sequence LVFLLLATLFSALAGLPWSLY description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 47) chain E residue 171-191 type LIPID sequence FVVTQCILLPVSSLLLYIIKI description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 48) chain E residue 196-216 type LIPID sequence FFIYAWLFTLVVSLVLVTIYA description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 49) chain E residue 348-368 type LIPID sequence NIIISQMNSFLCFFLFAVLIG description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 50) chain E residue 383-405 type LIPID sequence PTLIGLLIIFQFIFSPYNEVLSF description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 51) chain H residue 661 type LIPID sequence C description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 52) chain I residue 661 type LIPID sequence C description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 196-216 type LIPID sequence FFIYAWLFTLVVSLVLVTIYA description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 348-368 type LIPID sequence NIIISQMNSFLCFFLFAVLIG description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 383-405 type LIPID sequence PTLIGLLIIFQFIFSPYNEVLSF description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 56) chain B residue 19-39 type LIPID sequence IFGAVLLFSWTVYLWETFLAQ description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 57) chain B residue 82-102 type LIPID sequence GLYSETEGTLILLFGGIPYLW description S-farnesyl cysteine => ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603 source Swiss-Prot : SWS_FT_FI2 58) chain A residue 335 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 59) chain E residue 335 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 60) chain E residue 339 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 61) chain E residue 415 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 62) chain A residue 339 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 63) chain A residue 415 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 64) chain B residue 335 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 65) chain B residue 339 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 66) chain B residue 415 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 67) chain D residue 335 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 68) chain D residue 339 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 69) chain D residue 415 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 70) chain A residue 40-81 type TOPO_DOM sequence RQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSF WS description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 71) chain D residue 145-170 type TOPO_DOM sequence NTFVIEEKHGFNQQTLGFFMKDAIKK description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 72) chain D residue 217-347 type TOPO_DOM sequence DYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVE GSKRSSHSNAYFYGFKRIVLFDTLLEQGCKNEEVLAVLGH ALGHWKLGHTVK description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 73) chain E residue 40-81 type TOPO_DOM sequence RQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSF WS description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 74) chain E residue 145-170 type TOPO_DOM sequence NTFVIEEKHGFNQQTLGFFMKDAIKK description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 75) chain E residue 217-347 type TOPO_DOM sequence DYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVE GSKRSSHSNAYFYGFKRIVLFDTLLEGCKNEEVLAVLGHA LGHWKLGHTVK description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 76) chain A residue 145-170 type TOPO_DOM sequence NTFVIEEKHGFNQQTLGFFMKDAIKK description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 77) chain A residue 217-347 type TOPO_DOM sequence DYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVE GSKRSSHSNAYFYGFKRIVLFDTLLEQGCKNEEVLAVLGH ALGHWKLGHTVK description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 78) chain B residue 40-81 type TOPO_DOM sequence RQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSF WS description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 79) chain B residue 145-170 type TOPO_DOM sequence NTFVIEEKHGFNQQTLGFFMKDAIKK description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 80) chain B residue 217-347 type TOPO_DOM sequence DYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVE GSKRSSHSNAYFYGFKRIVLFDTLLEQGCKNEEVLAVLGH ALGHWKLGHTVK description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 81) chain D residue 40-81 type TOPO_DOM sequence RQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSF WS description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 82) chain A residue 336 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI4 83) chain B residue 336 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI4 84) chain D residue 336 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI4 85) chain E residue 336 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links