eF-site ID 1nt0-AG PDB Code 1nt0 Chain A, G click to enlarge Title Crystal structure of the CUB1-EGF-CUB2 region of MASP2 Classification HYDROLASE, SUGAR BINDING PROTEIN Compound mannose-binding protein associated serine protease-2 Source Rattus norvegicus (Rat) (MASP2_RAT) Sequence A:  EPVFGRLVSPGFPEKYGNHQDRSWTLTAPPGFRLRLYFTH FNLELSYRCEYDFVKLTSGTKVLATLCGQESTDTERAPGN DTFYSLGPSLKVTFHSDYPFTGFEAFYAAEDVDECRPCDH YCHXYLGGYYCSCRVGYILHQNKHTCSALCSGQVFTGRSG FLSSPEYPQPYPKLSSCAYNIRLEEGFSITLDFVESFDVE MHCDSLKIQTDKREYGPFCGKTLPPRIETDSNKVTITFTT DESGNHTGWKIHYTSTA G:  EPVFGRLVSPGFPEKYGNHQDRSWTLTAPPGFRLRLYFTH FNLELSYRCEYDFVKLTSGTKVLATLCGQESTDTERAPGN DTFYSLGPSLKVTFHSDYPFTGFEAFYAAEDVDECRPCDH YCHXYLGGYYCSCRVGYILHQNKHTCSALCSGQVFTGRSG FLSSPEYPQPYPKLSSCAYNIRLEEGFSITLDFVESFDVE MHCDSLKIQTDKREYGPFCGKTLPPRIETDSNKVTITFTT DESGNHTGWKIHYTSTA Description (1)  mannose-binding protein associated serine protease-2 Functional site 1) chain A residue 55 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 2) chain G residue 110 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 3) chain G residue 111 type BINDING sequence F description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 4) chain G residue 150 type BINDING sequence V description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 5) chain A residue 63 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 6) chain A residue 108 type BINDING sequence F description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 7) chain A residue 110 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 8) chain A residue 111 type BINDING sequence F description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 9) chain A residue 150 type BINDING sequence V description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 10) chain G residue 55 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 11) chain G residue 63 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 12) chain G residue 108 type BINDING sequence F description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 147 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI2 14) chain G residue 147 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI2 15) chain A residue 146 type MOD_RES sequence C description (3R)-3-hydroxyasparagine => ECO:0000269|PubMed:12743029 source Swiss-Prot : SWS_FT_FI3 16) chain G residue 146 type MOD_RES sequence C description (3R)-3-hydroxyasparagine => ECO:0000269|PubMed:12743029 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 91 type CARBOHYD sequence G description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12743029 source Swiss-Prot : SWS_FT_FI4 18) chain G residue 91 type CARBOHYD sequence G description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12743029 source Swiss-Prot : SWS_FT_FI4 19) chain A residue 273 type CARBOHYD sequence H description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 20) chain G residue 273 type CARBOHYD sequence H description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 21) chain A residue 137-148 type prosite sequence CHXYLGGYYCSC description ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. ChNylggYyCsC source prosite : PS00010 22) chain A residue 146-161 type prosite sequence CSCRVGYILHQNKHTC description EGF_2 EGF-like domain signature 2. CsCrvGYilhqnkhtC source prosite : PS01186 23) chain A residue 119-146 type prosite sequence DVDECRPCDHYCHXYLGGYYC description EGF_CA Calcium-binding EGF-like domain signature. DvDECrtslgdsvp.....Cdhy....ChNylggYyC source prosite : PS01187

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