eF-site ID 6sh2-.AAA PDB Code 6sh2 Chain AAA click to enlarge Title Crystal structure of human neprilysin E584D in complex with C-type natriuretic peptide. Classification PEPTIDE BINDING PROTEIN Compound Neprilysin Source (6SH2) Sequence AAA:  GICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKR NVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQ KAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENW EQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVN HVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVAR LIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRN DPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTV NISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWR FIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANY VNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQT LDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLN NEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDE WISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLN YGGIGMVIGHDITHGFDDNGRNFNKDGDLVDWWTQQSASN FKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGG LGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVW CGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFH CRKNSYMNPEKKCRVW Description Functional site 1) chain AAA residue 284 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519 source Swiss-Prot : SWS_FT_FI6 2) chain AAA residue 324 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10669592, ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566 source Swiss-Prot : SWS_FT_FI7 3) chain AAA residue 627 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10669592, ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566, ECO:0000269|PubMed:22766194 source Swiss-Prot : SWS_FT_FI8 4) chain AAA residue 583 type catalytic sequence H description 623 source MCSA : MCSA1 5) chain AAA residue 584 type catalytic sequence D description 623 source MCSA : MCSA1 6) chain AAA residue 587 type catalytic sequence H description 623 source MCSA : MCSA1 7) chain AAA residue 646 type catalytic sequence E description 623 source MCSA : MCSA1 8) chain AAA residue 650 type catalytic sequence D description 623 source MCSA : MCSA1 9) chain AAA residue 711 type catalytic sequence H description 623 source MCSA : MCSA1 10) chain AAA residue 717 type catalytic sequence R description 623 source MCSA : MCSA1 11) chain AAA residue 584 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095 source Swiss-Prot : SWS_FT_FI1 12) chain AAA residue 650 type ACT_SITE sequence D description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000269|PubMed:8168535 source Swiss-Prot : SWS_FT_FI2 13) chain AAA residue 102 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P07861 source Swiss-Prot : SWS_FT_FI3 14) chain AAA residue 587 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233 source Swiss-Prot : SWS_FT_FI4 15) chain AAA residue 646 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233 source Swiss-Prot : SWS_FT_FI4 16) chain AAA residue 583 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233 source Swiss-Prot : SWS_FT_FI4 17) chain AAA residue 144 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10669592, ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566 source Swiss-Prot : SWS_FT_FI5

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