eF-site ID 3s33-ABC PDB Code 3s33 Chain A, B, C click to enlarge Title Structure of Thermus thermophilus cytochrome ba3 oxidase 10s after Xe depressurization Classification OXIDOREDUCTASE Compound Cytochrome c oxidase subunit 1 Source null (COXA_THET8) Sequence A:  SEISRVYEAYPEKKATLYFLVLGFLALIVGSLFGPFQALN YGNVDAYPLLKRLLPFVQSYYQGLTLHGVLNAIVFTQLFA QAIMVYLPARELNMRPNMGLMWLSWWMAFIGLVVAALPLL ANEATVLYTFYPPLKGHWAFYLGASVFVLSTWVSIYIVLD LWRRWKAANPGKVTPLVTYMAVVFWLMWFLASLGLVLEAV LFLLPWSFGLVEGVDPLVARTLFWWTGHPIVYFWLLPAYA IIYTILPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQF ADPGIDPTWKMIHSVLTLFVAVPSLMTAFTVAASLEFAGR LRGGRGLFGWIRALPWDNPAFVAPVLGLLGFIPGGAGGIV NASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLL PNLTGKPISDAQRRLGLAVVWLWFLGMMIMAVGLHWAGLL NVPRRAYIAQVPDAYPHAAVPMVFNVLAGIVLLVALLLFI YGLFSVLLSRERKPELAEAPLPFAEVISGPEDRRLVLAMD RIGFWFAVAAILVVLAYGPTLVQLFGHLNPVPGWRLW B:  DEHKAHKAILAYEKGWLAFSLAMLFVFIALIAYTLATHTA GVIPAGKLERVDPTTVRQEGPWADPAQAVVQTGPNQYTVY VLAFAFGYQPNPIEVPQGAEIVFKITSPDVIHGFHVEGTN INVEVLPGEVSTVRYTFKRPGEYRIICNQYCGLGHQNMFG TIVVKE C:  EEKPKGALAVILVLTLTILVFWLGVYAVFFARG Description Functional site 1) chain A residue 233 type sequence H description BINDING SITE FOR RESIDUE CU A 803 source : AC1 2) chain A residue 282 type sequence H description BINDING SITE FOR RESIDUE CU A 803 source : AC1 3) chain A residue 283 type sequence H description BINDING SITE FOR RESIDUE CU A 803 source : AC1 4) chain A residue 36 type sequence S description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 5) chain A residue 39 type sequence G description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 6) chain A residue 40 type sequence P description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 7) chain A residue 42 type sequence Q description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 8) chain A residue 43 type sequence A description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 9) chain A residue 46 type sequence Y description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 10) chain A residue 65 type sequence Y description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 11) chain A residue 69 type sequence L description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 12) chain A residue 72 type sequence H description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 13) chain A residue 76 type sequence N description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 14) chain A residue 77 type sequence A description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 15) chain A residue 132 type sequence L description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 16) chain A residue 133 type sequence Y description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 17) chain A residue 385 type sequence F description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 18) chain A residue 386 type sequence H description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 19) chain A residue 389 type sequence V description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 20) chain A residue 390 type sequence A description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 21) chain A residue 394 type sequence T description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 22) chain A residue 428 type sequence W description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 23) chain A residue 432 type sequence M description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 24) chain A residue 449 type sequence R description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 25) chain A residue 450 type sequence R description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 26) chain A residue 451 type sequence A description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 27) chain A residue 477 type sequence L description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 28) chain A residue 133 type sequence Y description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 29) chain A residue 229 type sequence W description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 30) chain A residue 236 type sequence V description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 31) chain A residue 237 type sequence Y description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 32) chain A residue 239 type sequence W description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 33) chain A residue 282 type sequence H description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 34) chain A residue 283 type sequence H description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 35) chain A residue 309 type sequence S description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 36) chain A residue 313 type sequence A description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 37) chain A residue 317 type sequence A description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 38) chain A residue 335 type sequence W description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 39) chain A residue 350 type sequence V description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 40) chain A residue 353 type sequence L description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 41) chain A residue 354 type sequence L description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 42) chain A residue 356 type sequence F description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 43) chain A residue 360 type sequence G description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 44) chain A residue 363 type sequence G description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 45) chain A residue 366 type sequence N description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 46) chain A residue 367 type sequence A description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 47) chain A residue 372 type sequence D description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 48) chain A residue 376 type sequence H description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 49) chain A residue 381 type sequence V description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 50) chain A residue 384 type sequence H description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 51) chain A residue 385 type sequence F description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 52) chain A residue 388 type sequence Q description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 53) chain A residue 389 type sequence V description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 54) chain A residue 449 type sequence R description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 55) chain B residue 114 type sequence H description BINDING SITE FOR RESIDUE CUA B 802 source : AC4 56) chain B residue 149 type sequence C description BINDING SITE FOR RESIDUE CUA B 802 source : AC4 57) chain B residue 151 type sequence Q description BINDING SITE FOR RESIDUE CUA B 802 source : AC4 58) chain B residue 153 type sequence C description BINDING SITE FOR RESIDUE CUA B 802 source : AC4 59) chain B residue 157 type sequence H description BINDING SITE FOR RESIDUE CUA B 802 source : AC4 60) chain B residue 160 type sequence M description BINDING SITE FOR RESIDUE CUA B 802 source : AC4 61) chain A residue 232 type sequence G description BINDING SITE FOR RESIDUE XE A 563 source : AC5 62) chain A residue 228 type sequence F description BINDING SITE FOR RESIDUE XE A 567 source : AC6 63) chain A residue 229-283 type prosite sequence WWTGHPIVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLA FLLFLLLSTPVGFHH description COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WWTGHPiVyfwllpayaiiytilpkqaggklvsdpmarlafllflllstpvgf..HH source prosite : PS00077 64) chain A residue 283 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI4 65) chain A residue 282 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI4 66) chain A residue 237 type CROSSLNK sequence Y description 1'-histidyl-3'-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI5 67) chain A residue 233 type CROSSLNK sequence H description 1'-histidyl-3'-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI5 68) chain B residue 112-160 type prosite sequence VIHGFHVEGTNINVEVLPGEVSTVRYTFKRPGEYRIICNQ YCGLGHQNM description COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHgfhvegtninvevlpgevstvrytfkrpgeyrii......CnqyCglgHqnM source prosite : PS00078 69) chain B residue 86 type catalytic sequence F description 735 source MCSA : MCSA1 70) chain B residue 88 type catalytic sequence F description 735 source MCSA : MCSA1 71) chain A residue 384 type catalytic sequence H description 735 source MCSA : MCSA1 72) chain A residue 385 type catalytic sequence F description 735 source MCSA : MCSA1 73) chain A residue 386 type catalytic sequence H description 735 source MCSA : MCSA1 74) chain A residue 449 type catalytic sequence R description 735 source MCSA : MCSA1 75) chain A residue 450 type catalytic sequence R description 735 source MCSA : MCSA1 76) chain C residue 4-34 type TRANSMEM sequence KPKGALAVILVLTLTILVFWLGVYAVFFARG description Helical source Swiss-Prot : SWS_FT_FI1 77) chain A residue 74-94 type TRANSMEM sequence VLNAIVFTQLFAQAIMVYLPA description Helical source Swiss-Prot : SWS_FT_FI1 78) chain A residue 105-125 type TRANSMEM sequence LMWLSWWMAFIGLVVAALPLL description Helical source Swiss-Prot : SWS_FT_FI1 79) chain A residue 144-164 type TRANSMEM sequence AFYLGASVFVLSTWVSIYIVL description Helical source Swiss-Prot : SWS_FT_FI1 80) chain A residue 187-207 type TRANSMEM sequence VVFWLMWFLASLGLVLEAVLF description Helical source Swiss-Prot : SWS_FT_FI1 81) chain A residue 227-247 type TRANSMEM sequence LFWWTGHPIVYFWLLPAYAII description Helical source Swiss-Prot : SWS_FT_FI1 82) chain A residue 267-287 type TRANSMEM sequence LAFLLFLLLSTPVGFHHQFAD description Helical source Swiss-Prot : SWS_FT_FI1 83) chain A residue 300-320 type TRANSMEM sequence VLTLFVAVPSLMTAFTVAASL description Helical source Swiss-Prot : SWS_FT_FI1 84) chain A residue 345-365 type TRANSMEM sequence AFVAPVLGLLGFIPGGAGGIV description Helical source Swiss-Prot : SWS_FT_FI1 85) chain A residue 385-405 type TRANSMEM sequence FHLQVASLVTLTAMGSLYWLL description Helical source Swiss-Prot : SWS_FT_FI1 86) chain A residue 420-440 type TRANSMEM sequence LGLAVVWLWFLGMMIMAVGLH description Helical source Swiss-Prot : SWS_FT_FI1 87) chain A residue 471-491 type TRANSMEM sequence VLAGIVLLVALLLFIYGLFSV description Helical source Swiss-Prot : SWS_FT_FI1 88) chain A residue 527-547 type TRANSMEM sequence IGFWFAVAAILVVLAYGPTLV description Helical source Swiss-Prot : SWS_FT_FI1 89) chain A residue 386 type TOPO_DOM sequence H description Periplasmic source Swiss-Prot : SWS_FT_FI2 90) chain B residue 39-168 type TOPO_DOM sequence THTAGVIPAGKLERVDPTTVRQEGPWADPAQAVVQTGPNQ YTVYVLAFAFGYQPNPIEVPQGAEIVFKITSPDVIHGFHV EGTNINVEVLPGEVSTVRYTFKRPGEYRIICNQYCGLGHQ NMFGTIVVKE description Periplasmic source Swiss-Prot : SWS_FT_FI2 91) chain A residue 384 type TOPO_DOM sequence H description Periplasmic source Swiss-Prot : SWS_FT_FI2 92) chain B residue 153 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI3 93) chain B residue 157 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 94) chain B residue 114 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 95) chain B residue 149 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI3

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