eF-site ID 1oco-A PDB Code 1oco Chain A click to enlarge Title BOVINE HEART CYTOCHROME C OXIDASE IN CARBON MONOXIDE-BOUND STATE Classification OXIDOREDUCTASE Compound CYTOCHROME C OXIDASE Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAE LGQPGTLLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGN WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEA GAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG AINFITTIINMKPPAMSQYQTPLFVWSVMITAVLLLLSLP VLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH PEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSI GFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV FSWLATLHGGNIKWSPAMMWALGFIFLFTVGGLTGIVLAN SSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF SGYTLNDTWAKIHFAIMFVGVNMTFFPQHFLGLSGMPRRY SDYPDAYTMWNTISSMGSFISLTAVMLMVFIIWEAFASKR EVLTVDLTTTNLEWLNGCPPPYHTFEEPTYVNLK Description (1)  CYTOCHROME C OXIDASE, HEME-A, CARBON MONOXIDE Functional site 1) chain A residue 240 type sequence H description BINDING SITE FOR RESIDUE CU A 517 source : AC1 2) chain A residue 290 type sequence H description BINDING SITE FOR RESIDUE CU A 517 source : AC1 3) chain A residue 291 type sequence H description BINDING SITE FOR RESIDUE CU A 517 source : AC1 4) chain A residue 368 type sequence H description BINDING SITE FOR RESIDUE MG A 518 source : AC2 5) chain A residue 369 type sequence D description BINDING SITE FOR RESIDUE MG A 518 source : AC2 6) chain A residue 40 type sequence E description BINDING SITE FOR RESIDUE NA A 519 source : AC3 7) chain A residue 43 type sequence Q description BINDING SITE FOR RESIDUE NA A 519 source : AC3 8) chain A residue 45 type sequence G description BINDING SITE FOR RESIDUE NA A 519 source : AC3 9) chain A residue 441 type sequence S description BINDING SITE FOR RESIDUE NA A 519 source : AC3 10) chain A residue 27 type sequence G description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 11) chain A residue 34 type sequence S description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 12) chain A residue 37 type sequence I description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 13) chain A residue 38 type sequence R description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 14) chain A residue 54 type sequence Y description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 15) chain A residue 61 type sequence H description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 16) chain A residue 62 type sequence A description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 17) chain A residue 65 type sequence M description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 18) chain A residue 70 type sequence V description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 19) chain A residue 125 type sequence G description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 20) chain A residue 126 type sequence W description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 21) chain A residue 371 type sequence Y description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 22) chain A residue 377 type sequence F description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 23) chain A residue 378 type sequence H description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 24) chain A residue 381 type sequence L description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 25) chain A residue 382 type sequence S description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 26) chain A residue 386 type sequence V description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 27) chain A residue 390 type sequence M description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 28) chain A residue 425 type sequence F description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 29) chain A residue 428 type sequence Q description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 30) chain A residue 438 type sequence R description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 31) chain A residue 439 type sequence R description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 32) chain A residue 440 type sequence Y description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 33) chain A residue 468 type sequence M description BINDING SITE FOR RESIDUE HEA A 515 source : BC4 34) chain A residue 126 type sequence W description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 35) chain A residue 243 type sequence V description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 36) chain A residue 244 type sequence Y description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 37) chain A residue 290 type sequence H description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 38) chain A residue 291 type sequence H description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 39) chain A residue 309 type sequence T description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 40) chain A residue 312 type sequence I description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 41) chain A residue 317 type sequence G description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 42) chain A residue 352 type sequence G description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 43) chain A residue 355 type sequence G description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 44) chain A residue 356 type sequence I description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 45) chain A residue 358 type sequence L description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 46) chain A residue 359 type sequence A description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 47) chain A residue 364 type sequence D description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 48) chain A residue 368 type sequence H description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 49) chain A residue 376 type sequence H description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 50) chain A residue 377 type sequence F description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 51) chain A residue 380 type sequence V description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 52) chain A residue 381 type sequence L description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 53) chain A residue 438 type sequence R description BINDING SITE FOR RESIDUE HEA A 516 source : BC5 54) chain A residue 240 type sequence H description BINDING SITE FOR RESIDUE CMO A 520 source : BC6 55) chain A residue 290 type sequence H description BINDING SITE FOR RESIDUE CMO A 520 source : BC6 56) chain A residue 291 type sequence H description BINDING SITE FOR RESIDUE CMO A 520 source : BC6 57) chain A residue 270-286 type TRANSMEM sequence YMGMVWAMMSIGFLGFI description Helical; Name=VII => ECO:0000269|PubMed:27605664 source Swiss-Prot : SWS_FT_FI10 58) chain A residue 299-327 type TRANSMEM sequence VDTRAYFTSATMIIAIPTGVKVFSWLATL description Helical; Name=VIII => ECO:0000269|PubMed:27605664 source Swiss-Prot : SWS_FT_FI11 59) chain A residue 328-335 type TOPO_DOM sequence HGGNIKWS description Mitochondrial matrix => ECO:0000269|PubMed:27605664 source Swiss-Prot : SWS_FT_FI12 60) chain A residue 336-357 type TRANSMEM sequence PAMMWALGFIFLFTVGGLTGIV description Helical; Name=IX => ECO:0000269|PubMed:27605664 source Swiss-Prot : SWS_FT_FI13 61) chain A residue 358-370 type TOPO_DOM sequence LANSSLDIVLHDT description Mitochondrial intermembrane => ECO:0000269|PubMed:27605664 source Swiss-Prot : SWS_FT_FI14 62) chain A residue 434-446 type TOPO_DOM sequence SGMPRRYSDYPDA description Mitochondrial intermembrane => ECO:0000269|PubMed:27605664 source Swiss-Prot : SWS_FT_FI14 63) chain A residue 371-400 type TRANSMEM sequence YYVVAHFHYVLSMGAVFAIMGGFVHWFPLF description Helical; Name=X => ECO:0000269|PubMed:27605664 source Swiss-Prot : SWS_FT_FI15 64) chain A residue 407-433 type TRANSMEM sequence DTWAKIHFAIMFVGVNMTFFPQHFLGL description Helical; Name=XI => ECO:0000269|PubMed:27605664 source Swiss-Prot : SWS_FT_FI16 65) chain A residue 447-478 type TRANSMEM sequence YTMWNTISSMGSFISLTAVMLMVFIIWEAFAS description Helical; Name=XII => ECO:0000269|PubMed:27605664 source Swiss-Prot : SWS_FT_FI17 66) chain A residue 40 type BINDING sequence E description BINDING => ECO:0000269|PubMed:27605664, ECO:0000305|PubMed:23537388 source Swiss-Prot : SWS_FT_FI18 67) chain A residue 441 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27605664, ECO:0000305|PubMed:23537388 source Swiss-Prot : SWS_FT_FI18 68) chain A residue 45 type BINDING sequence G description BINDING => ECO:0000269|PubMed:27605664, ECO:0000305|PubMed:23537388 source Swiss-Prot : SWS_FT_FI18 69) chain A residue 61 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158 source Swiss-Prot : SWS_FT_FI19 70) chain A residue 376 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158 source Swiss-Prot : SWS_FT_FI19 71) chain A residue 378 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158 source Swiss-Prot : SWS_FT_FI19 72) chain A residue 369 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158 source Swiss-Prot : SWS_FT_FI20 73) chain A residue 240 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158 source Swiss-Prot : SWS_FT_FI20 74) chain A residue 290 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158 source Swiss-Prot : SWS_FT_FI20 75) chain A residue 291 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158 source Swiss-Prot : SWS_FT_FI20 76) chain A residue 368 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158 source Swiss-Prot : SWS_FT_FI20 77) chain A residue 244 type BINDING sequence Y description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI21 78) chain A residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2165784 source Swiss-Prot : SWS_FT_FI22 79) chain A residue 240 type CROSSLNK sequence H description 1'-histidyl-3'-tyrosine (His-Tyr) => ECO:0000269|PubMed:10338009 source Swiss-Prot : SWS_FT_FI23 80) chain A residue 244 type CROSSLNK sequence Y description 1'-histidyl-3'-tyrosine (His-Tyr) => ECO:0000269|PubMed:10338009 source Swiss-Prot : SWS_FT_FI23 81) chain A residue 61 type catalytic sequence H description 124 source MCSA : MCSA1 82) chain A residue 91 type catalytic sequence D description 124 source MCSA : MCSA1 83) chain A residue 126 type catalytic sequence W description 124 source MCSA : MCSA1 84) chain A residue 156 type catalytic sequence S description 124 source MCSA : MCSA1 85) chain A residue 157 type catalytic sequence S description 124 source MCSA : MCSA1 86) chain A residue 240 type catalytic sequence H description 124 source MCSA : MCSA1 87) chain A residue 242 type catalytic sequence E description 124 source MCSA : MCSA1 88) chain A residue 244 type catalytic sequence Y description 124 source MCSA : MCSA1 89) chain A residue 255 type catalytic sequence S description 124 source MCSA : MCSA1 90) chain A residue 290 type catalytic sequence H description 124 source MCSA : MCSA1 91) chain A residue 291 type catalytic sequence H description 124 source MCSA : MCSA1 92) chain A residue 316 type catalytic sequence T description 124 source MCSA : MCSA1 93) chain A residue 319 type catalytic sequence K description 124 source MCSA : MCSA1 94) chain A residue 438 type catalytic sequence R description 124 source MCSA : MCSA1 95) chain A residue 236-291 type prosite sequence WFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVW AMMSIGFLGFIVWAHH description COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyililpgfgmishivtyysgkkepfgymgmvwammsigflgfivwa.HH source prosite : PS00077

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