eF-site ID 5v48-AB PDB Code 5v48 Chain A, B click to enlarge Title Soluble rabbit neprilysin in complex with thiorphan Classification HYDROLASE Compound Neprilysin Source (NEP_RABIT) Sequence A:  GICKSSDCIKSAARLIQNMDATAEPCTDFFKYACGGWLKR NVIPETSSRYSNFDILRDELEVILKDVLQEPKTEDIVAVQ KAKTLYRSCVNETAIDSRGGQPLLKLLPDVYGWPVATQNW EQTYGTSWSAEKSIAQLNSKYGKKVLINFFVGTDDKNSMN HIIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMIAVAK LIRQEEGLPIDENQISVEMNKVMELEKEIANATTKSEDRN DPMLLYNKMTLAQIQNNFSLEINGKPFSWSNFTNEIMSTV NINIPNEEDVVVYAPEYLIKLKPILTKYSPRDLQNLMSWR FIMDLVSSLSRTYKDSRNAFRKALYGTTSESATWRRCANY VNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQT LDDLTWMDAETKKKAEEKALAIKERIGYPDDIVSNDNKLN NEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDE WITGAAIVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLN YGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSANN FKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGG IGQAYRAYQNYVKKNGEEKLLPGIDLNHKQLFFLNFAQVW CGTYRPEYAVNSIKTDVHSPGNFRIIGSLQNSVEFSEAFQ CPKNSYMNPEKKCRVW B:  GICKSSDCIKSAARLIQNMDATAEPCTDFFKYACGGWLKR NVIPETSSRYSNFDILRDELEVILKDVLQEPKTEDIVAVQ KAKTLYRSCVNETAIDSRGGQPLLKLLPDVYGWPVATQNW EQTYGTSWSAEKSIAQLNSKYGKKVLINFFVGTDDKNSMN HIIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMIAVAK LIRQEEGLPIDENQISVEMNKVMELEKEIANATTKSEDRN DPMLLYNKMTLAQIQNNFSLEINGKPFSWSNFTNEIMSTV NINIPNEEDVVVYAPEYLIKLKPILTKYSPRDLQNLMSWR FIMDLVSSLSRTYKDSRNAFRKALYGTTSESATWRRCANY VNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQT LDDLTWMDAETKKKAEEKALAIKERIGYPDDIVSNDNKLN NEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDE WITGAAIVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLN YGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSANN FKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGG IGQAYRAYQNYVKKNGEEKLLPGIDLNHKQLFFLNFAQVW CGTYRPEYAVNSIKTDVHSPGNFRIIGSLQNSVEFSEAFQ CPKNSYMNPEKKCRVW Description Functional site 1) chain A residue 585 type ACT_SITE sequence E description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095 source Swiss-Prot : SWS_FT_FI1 2) chain B residue 585 type ACT_SITE sequence E description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095 source Swiss-Prot : SWS_FT_FI1 3) chain A residue 651 type ACT_SITE sequence D description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01233 source Swiss-Prot : SWS_FT_FI2 4) chain B residue 651 type ACT_SITE sequence D description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01233 source Swiss-Prot : SWS_FT_FI2 5) chain A residue 103 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P07861 source Swiss-Prot : SWS_FT_FI3 6) chain B residue 103 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P07861 source Swiss-Prot : SWS_FT_FI3 7) chain A residue 581-590 type prosite sequence VIGHEITHGF description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIGHEITHGF source prosite : PS00142 8) chain A residue 628 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine source Swiss-Prot : SWS_FT_FI8 9) chain B residue 628 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine source Swiss-Prot : SWS_FT_FI8 10) chain A residue 584 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000305|PubMed:3162886 source Swiss-Prot : SWS_FT_FI4 11) chain A residue 588 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000305|PubMed:3162886 source Swiss-Prot : SWS_FT_FI4 12) chain B residue 584 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000305|PubMed:3162886 source Swiss-Prot : SWS_FT_FI4 13) chain B residue 588 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000305|PubMed:3162886 source Swiss-Prot : SWS_FT_FI4 14) chain A residue 647 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233 source Swiss-Prot : SWS_FT_FI5 15) chain B residue 647 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233 source Swiss-Prot : SWS_FT_FI5 16) chain A residue 145 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P08473 source Swiss-Prot : SWS_FT_FI6 17) chain A residue 311 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P08473 source Swiss-Prot : SWS_FT_FI6 18) chain A residue 325 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P08473 source Swiss-Prot : SWS_FT_FI6 19) chain B residue 145 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P08473 source Swiss-Prot : SWS_FT_FI6 20) chain B residue 311 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P08473 source Swiss-Prot : SWS_FT_FI6 21) chain B residue 325 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P08473 source Swiss-Prot : SWS_FT_FI6 22) chain A residue 285 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 23) chain B residue 285 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7

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