eF-site ID 2ypt-E PDB Code 2ypt Chain E 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 null (LMNA_HUMAN) Sequence E:  LWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTT HVPPELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSETEG TLILLFGGIPYLWRLSGRPEYEITQSLVFLLLATLFSALA GLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIKKFVVTQCI LLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYAD YIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVEG SKRSSHSNAYFYGFKRIVLFDTLLEGCKNEEVLAVLGHAL GHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAFG FYDSQPTLIGLLIIFQFIFSPYNEVLSFCLTVLSRRFEFQ ADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSMWHY SHPPLLERLQALKT Description (1)  CAAX PRENYL PROTEASE 1 HOMOLOG (E.C.3.4.24.84), PRELAMIN-A/C Functional site 1) chain E residue 335 type sequence H description BINDING SITE FOR RESIDUE ZN E 600 source : AC4 2) chain E residue 339 type sequence H description BINDING SITE FOR RESIDUE ZN E 600 source : AC4 3) chain E residue 415 type sequence E description BINDING SITE FOR RESIDUE ZN E 600 source : AC4 4) 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 5) 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 6) 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 7) 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 8) 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 9) 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 10) 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 11) 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 12) 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 13) 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 14) chain E residue 40-81 type TOPO_DOM sequence RQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSF WS description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 15) chain E residue 145-170 type TOPO_DOM sequence NTFVIEEKHGFNQQTLGFFMKDAIKK description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 16) chain E residue 217-347 type TOPO_DOM sequence DYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVE GSKRSSHSNAYFYGFKRIVLFDTLLEGCKNEEVLAVLGHA LGHWKLGHTVK description Nuclear => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 17) chain E residue 336 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI4 18) chain E residue 335 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 19) chain E residue 339 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5 20) chain E residue 415 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23539603 source Swiss-Prot : SWS_FT_FI5

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