eF-site ID 6sh1-.CCC PDB Code 6sh1 Chain CCC click to enlarge Title Crystal structure of substrate-free human neprilysin E584D. Classification PEPTIDE BINDING PROTEIN Compound Neprilysin Source (NEP_HUMAN) Sequence CCC:  GICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKR NVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQ KAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENW EQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVN HVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVAR LIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRN DPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTV NISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWR FIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANY VNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQT LDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLN NEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDE WISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLN YGGIGMVIGHDITHGFDDNGRNFNKDGDLVDWWTQQSASN FKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGG LGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVW CGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFH CRKNSYMNPEKKCRVW Description Functional site 1) chain CCC residue 284 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519 source Swiss-Prot : SWS_FT_FI6 2) chain CCC 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 CCC 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 CCC residue 650 type catalytic sequence D description 623 source MCSA : MCSA2 5) chain CCC residue 583 type catalytic sequence H description 623 source MCSA : MCSA2 6) chain CCC residue 584 type catalytic sequence D description 623 source MCSA : MCSA2 7) chain CCC residue 587 type catalytic sequence H description 623 source MCSA : MCSA2 8) chain CCC residue 646 type catalytic sequence E description 623 source MCSA : MCSA2 9) chain CCC residue 711 type catalytic sequence H description 623 source MCSA : MCSA2 10) chain CCC residue 717 type catalytic sequence R description 623 source MCSA : MCSA2 11) chain CCC residue 583 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233 source Swiss-Prot : SWS_FT_FI4 12) chain CCC residue 587 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233 source Swiss-Prot : SWS_FT_FI4 13) chain CCC residue 646 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01233 source Swiss-Prot : SWS_FT_FI4 14) chain CCC 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 15) chain CCC 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 16) chain CCC residue 102 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P07861 source Swiss-Prot : SWS_FT_FI3 17) chain CCC 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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