eF-site ID 1kcw-A PDB Code 1kcw Chain A click to enlarge Title X-RAY CRYSTAL STRUCTURE OF HUMAN CERULOPLASMIN AT 3.0 ANGSTROMS Classification OXIDOREDUCTASE Compound CERULOPLASMIN Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence A:  KEKHYYIGIIETTWDYASDHGEKKLISVDTEHSNIYLQNG PDRIGRLYKKALYLQYTDETFRTTIEKPVWLGFLGPIIKA ETGDKVYVHLKNLASRPYTFHSHGITYYKEHEGAIYPDNT TDFQRADDKVYPGEQYTYMLLATEEQSPGEGDGNCVTRIY HSHIDAPKDIASGLIGPLIICKKDSLDKEKEKHIDREFVV MFSVVDENFSWYLEDNIKTYCSEPEKVDKDNEDFQESNRM YSVNGYTFGSLPGLSMCAEDRVKWYLFGMGNEVDVHAAFF HGQALTNKNYRIDTINLFPATLFDAYMVAQNPGEWMLSCQ NLNHLKAGLQAFFQVQECIRGKHVRHYYIAAEEIIWNYAP SGIDIFTKENLTAPGSDSAVFFEQGTTRIGGSYKKLVYRE YTDASFTNRKERGPEEEHLGILGPVIWAEVGDTIRVTFHN KGAYPLSIEPIGVRFNKNNEGTYYSPVPPSASHVAPTETF TYEWTVPKEVGPTNADPVCLAKMYYSAVDPTKDIFTGLIG PMKICKKGSLHANGRQKDVDKEFYLFPTVFDENESLLLED NIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLT MCKGDSVVWYLFSAGNEADVHGIYFSGNTYLWRGERRDTA NLFPQTSLTLHMWPDTEGTFNVECLTTDHYTGGMKQKYTV NQCRRQSEDSTFYLGERTYYIAAVEVEWDYSPQREWEKEL HHLQEQNVSNAFLDKGEFYIGSKYKKVVYRQYTDSTFRVP VERKAEEEHLGILGPQLHADVGDKVKIIFKNMATRPYSIH AHGVQTESSTVTPTLPGETLTYVWKIPERSGAGTEDSACI PWAYYSTVDQVKDLYSGLIGPLIVCRRPRRKLEFALLFLV FDENESWYLDDNIKTYSDHPEKVNKDDEEFIESNKMHAIN GRMFGNLQGLTMHVGDEVNWYLMGMGNEIDLHTVHFHGHS FQYKHRGVYSSDVFDIFPGTYQTLEMFPRTPGIWLLHCHV TDHIHAGMETTYTVLQN Description (1)  CERULOPLASMIN, OXYGEN ATOM Functional site 1) chain A residue 276 type sequence H description TYPE I CU BINDING SITE IN DOMAIN 2. AT BEST LEU 329 MAY HAVE VAN DER WAALS CONTACT WITH THE CU. source : CU1 2) chain A residue 319 type sequence C description TYPE I CU BINDING SITE IN DOMAIN 2. AT BEST LEU 329 MAY HAVE VAN DER WAALS CONTACT WITH THE CU. source : CU1 3) chain A residue 324 type sequence H description TYPE I CU BINDING SITE IN DOMAIN 2. AT BEST LEU 329 MAY HAVE VAN DER WAALS CONTACT WITH THE CU. source : CU1 4) chain A residue 329 type sequence L description TYPE I CU BINDING SITE IN DOMAIN 2. AT BEST LEU 329 MAY HAVE VAN DER WAALS CONTACT WITH THE CU. source : CU1 5) chain A residue 637 type sequence H description TYPE I CU BINDING SITE IN DOMAIN 4. source : CU2 6) chain A residue 680 type sequence C description TYPE I CU BINDING SITE IN DOMAIN 4. source : CU2 7) chain A residue 685 type sequence H description TYPE I CU BINDING SITE IN DOMAIN 4. source : CU2 8) chain A residue 690 type sequence M description TYPE I CU BINDING SITE IN DOMAIN 4. source : CU2 9) chain A residue 597 type sequence E description LABILE CU BINDING SITE IN DOMAIN 4. source : CU3 10) chain A residue 602 type sequence H description LABILE CU BINDING SITE IN DOMAIN 4. source : CU3 11) chain A residue 684 type sequence D description LABILE CU BINDING SITE IN DOMAIN 4. source : CU3 12) chain A residue 971 type sequence E description LABILE CU BINDING SITE IN DOMAIN 4. source : CU3 13) chain A residue 975 type sequence H description TYPE I CU BINDING SITE IN DOMAIN 6. source : CU4 14) chain A residue 1021 type sequence C description TYPE I CU BINDING SITE IN DOMAIN 6. source : CU4 15) chain A residue 1026 type sequence H description TYPE I CU BINDING SITE IN DOMAIN 6. source : CU4 16) chain A residue 1031 type sequence M description TYPE I CU BINDING SITE IN DOMAIN 6. source : CU4 17) chain A residue 272 type sequence E description LABILE CU BINDING SITE IN DOMAIN 6. source : CU5 18) chain A residue 935 type sequence E description LABILE CU BINDING SITE IN DOMAIN 6. source : CU5 19) chain A residue 940 type sequence H description LABILE CU BINDING SITE IN DOMAIN 6. source : CU5 20) chain A residue 1025 type sequence D description LABILE CU BINDING SITE IN DOMAIN 6. source : CU5 21) chain A residue 101 type sequence H description TRINUCLEAR CENTER. CU31 AND 32 ARE THE PAIR OF TYPE III CU AND CU34 IS THE TYPE II CU. O33 BRIDGES CU 31 - 32 AND O35 BRIDGES Y 107 - CU 34. source : TRI 22) chain A residue 103 type sequence H description TRINUCLEAR CENTER. CU31 AND 32 ARE THE PAIR OF TYPE III CU AND CU34 IS THE TYPE II CU. O33 BRIDGES CU 31 - 32 AND O35 BRIDGES Y 107 - CU 34. source : TRI 23) chain A residue 161 type sequence H description TRINUCLEAR CENTER. CU31 AND 32 ARE THE PAIR OF TYPE III CU AND CU34 IS THE TYPE II CU. O33 BRIDGES CU 31 - 32 AND O35 BRIDGES Y 107 - CU 34. source : TRI 24) chain A residue 163 type sequence H description TRINUCLEAR CENTER. CU31 AND 32 ARE THE PAIR OF TYPE III CU AND CU34 IS THE TYPE II CU. O33 BRIDGES CU 31 - 32 AND O35 BRIDGES Y 107 - CU 34. source : TRI 25) chain A residue 978 type sequence H description TRINUCLEAR CENTER. CU31 AND 32 ARE THE PAIR OF TYPE III CU AND CU34 IS THE TYPE II CU. O33 BRIDGES CU 31 - 32 AND O35 BRIDGES Y 107 - CU 34. source : TRI 26) chain A residue 980 type sequence H description TRINUCLEAR CENTER. CU31 AND 32 ARE THE PAIR OF TYPE III CU AND CU34 IS THE TYPE II CU. O33 BRIDGES CU 31 - 32 AND O35 BRIDGES Y 107 - CU 34. source : TRI 27) chain A residue 1020 type sequence H description TRINUCLEAR CENTER. CU31 AND 32 ARE THE PAIR OF TYPE III CU AND CU34 IS THE TYPE II CU. O33 BRIDGES CU 31 - 32 AND O35 BRIDGES Y 107 - CU 34. source : TRI 28) chain A residue 1022 type sequence H description TRINUCLEAR CENTER. CU31 AND 32 ARE THE PAIR OF TYPE III CU AND CU34 IS THE TYPE II CU. O33 BRIDGES CU 31 - 32 AND O35 BRIDGES Y 107 - CU 34. source : TRI 29) chain A residue 313-333 type prosite sequence GEWMLSCQNLNHLKAGLQAFF description MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF source prosite : PS00079 30) chain A residue 674-694 type prosite sequence GTFNVECLTTDHYTGGMKQKY description MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF source prosite : PS00079 31) chain A residue 1015-1035 type prosite sequence GIWLLHCHVTDHIHAGMETTY description MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF source prosite : PS00079 32) chain A residue 378 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI10 33) chain A residue 569 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI11 34) chain A residue 907 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI11 35) chain A residue 743 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW source Swiss-Prot : SWS_FT_FI12 36) chain A residue 101 type BINDING sequence H description type 2 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI2 37) chain A residue 978 type BINDING sequence H description type 2 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI2 38) chain A residue 103 type BINDING sequence H description type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI3 39) chain A residue 161 type BINDING sequence H description type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI3 40) chain A residue 163 type BINDING sequence H description type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI3 41) chain A residue 980 type BINDING sequence H description type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI3 42) chain A residue 1020 type BINDING sequence H description type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI3 43) chain A residue 1022 type BINDING sequence H description type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI3 44) chain A residue 319 type BINDING sequence C description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI4 45) chain A residue 324 type BINDING sequence H description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI4 46) chain A residue 637 type BINDING sequence H description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI4 47) chain A residue 680 type BINDING sequence C description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI4 48) chain A residue 685 type BINDING sequence H description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI4 49) chain A residue 690 type BINDING sequence M description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI4 50) chain A residue 1026 type BINDING sequence H description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI4 51) chain A residue 1031 type BINDING sequence M description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI4 52) chain A residue 276 type BINDING sequence H description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI4 53) chain A residue 398 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W source Swiss-Prot : SWS_FT_FI5 54) chain A residue 401 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W source Swiss-Prot : SWS_FT_FI5 55) chain A residue 598 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W source Swiss-Prot : SWS_FT_FI5 56) chain A residue 748 type BINDING sequence F description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W source Swiss-Prot : SWS_FT_FI5 57) chain A residue 757 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W source Swiss-Prot : SWS_FT_FI5 58) chain A residue 760 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W source Swiss-Prot : SWS_FT_FI5 59) chain A residue 936 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W source Swiss-Prot : SWS_FT_FI5 60) chain A residue 389 type BINDING sequence F description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W source Swiss-Prot : SWS_FT_FI5 61) chain A residue 1021 type BINDING sequence C description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI6 62) chain A residue 975 type BINDING sequence H description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI6 63) chain A residue 703 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI7 64) chain A residue 119 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI8 65) chain A residue 1020-1031 type prosite sequence HCHVTDHIHAGM description MULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvtdHihaGM source prosite : PS00080 66) chain A residue 48 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI1 67) chain A residue 109 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI1 68) chain A residue 124 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI1 69) chain A residue 127 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI1 70) chain A residue 128 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI1 71) chain A residue 237 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI1 72) chain A residue 36 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI1 73) chain A residue 45 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ source Swiss-Prot : SWS_FT_FI1

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