eF-site ID 3qjq-A PDB Code 3qjq Chain A click to enlarge Title The structure of and photolytic induced changes of carbon monoxide binding to the cytochrome ba3-oxidase from Thermus thermophilus Classification OXIDOREDUCTASE Compound Cytochrome c oxidase subunit 1 Source null (COXA_THET8) Sequence A:  VYEAYPEKKATLYFLVLGFLALIVGSLFGPFQALNYGNVD AYPLLKRLLPFVQSYYQGLTLHGVLNAIVFTQLFAQAIMV YLPARELNMRPNMGLMWLSWWMAFIGLVVAALPLLANEAT VLYTFYPPLKGHWAFYLGASVFVLSTWVSIYIVLDLWRRW KAANPGKVTPLVTYMAVVFWLMWFLASLGLVLEAVLFLLP WSFGLVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTI LPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQFADPGI DPTWKMIHSVLTLFVAVPSLMTAFTVAASLEFAGRLRGGR GLFGWIRALPWDNPAFVAPVLGLLGFIPGGAGGIVNASFT LDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTG KPISDAQRRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRR AYIAQVPDAYPHAAVPMVFNVLAGIVLLVALLLFIYGLFS VLLSRERKPELAEAPLPFAEVISGPEDRRLVLAMDRIGFW FAVAAILVVLAYGPTLVQLFGHLNPVPGWRLW Description Functional site 1) chain A residue 233 type sequence H description BINDING SITE FOR RESIDUE CU1 A 803 source : AC1 2) chain A residue 282 type sequence H description BINDING SITE FOR RESIDUE CU1 A 803 source : AC1 3) chain A residue 283 type sequence H description BINDING SITE FOR RESIDUE CU1 A 803 source : AC1 4) chain A residue 32 type sequence L 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 42 type sequence Q description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 7) chain A residue 46 type sequence Y description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 8) chain A residue 65 type sequence Y description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 9) chain A residue 69 type sequence L description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 10) chain A residue 72 type sequence H description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 11) chain A residue 76 type sequence N description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 12) chain A residue 133 type sequence Y description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 13) chain A residue 385 type sequence F description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 14) chain A residue 386 type sequence H description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 15) chain A residue 389 type sequence V description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 16) chain A residue 390 type sequence A description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 17) chain A residue 394 type sequence T description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 18) chain A residue 428 type sequence W description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 19) chain A residue 432 type sequence M description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 20) chain A residue 435 type sequence M description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 21) chain A residue 449 type sequence R description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 22) chain A residue 450 type sequence R description BINDING SITE FOR RESIDUE HEM A 800 source : AC2 23) chain A residue 133 type sequence Y description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 24) chain A residue 229 type sequence W description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 25) chain A residue 236 type sequence V description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 26) chain A residue 237 type sequence Y description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 27) chain A residue 239 type sequence W description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 28) chain A residue 282 type sequence H description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 29) chain A residue 309 type sequence S description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 30) chain A residue 310 type sequence L description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 31) chain A residue 313 type sequence A description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 32) chain A residue 336 type sequence I description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 33) chain A residue 353 type sequence L description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 34) chain A residue 356 type sequence F description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 35) chain A residue 363 type sequence G description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 36) chain A residue 366 type sequence N description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 37) chain A residue 367 type sequence A description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 38) chain A residue 372 type sequence D description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 39) chain A residue 376 type sequence H description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 40) chain A residue 381 type sequence V description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 41) chain A residue 384 type sequence H description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 42) chain A residue 385 type sequence F description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 43) chain A residue 388 type sequence Q description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 44) chain A residue 389 type sequence V description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 45) chain A residue 449 type sequence R description BINDING SITE FOR RESIDUE HAS A 801 source : AC3 46) chain A residue 233 type sequence H description BINDING SITE FOR RESIDUE CMO A 563 source : AC5 47) chain A residue 282 type sequence H description BINDING SITE FOR RESIDUE CMO A 563 source : AC5 48) chain A residue 283 type sequence H description BINDING SITE FOR RESIDUE CMO A 563 source : AC5 49) chain A residue 386 type MOD_RES sequence H description N-formylmethionine => ECO:0000269|PubMed:11152118 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 384 type MOD_RES sequence H description N-formylmethionine => ECO:0000269|PubMed:11152118 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 237 type CROSSLNK sequence Y description 1'-histidyl-3'-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI5 52) chain A residue 233 type CROSSLNK sequence H description 1'-histidyl-3'-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI5 53) 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 54) chain A residue 384 type catalytic sequence H description 735 source MCSA : MCSA1 55) chain A residue 385 type catalytic sequence F description 735 source MCSA : MCSA1 56) chain A residue 386 type catalytic sequence H description 735 source MCSA : MCSA1 57) chain A residue 449 type catalytic sequence R description 735 source MCSA : MCSA1 58) chain A residue 450 type catalytic sequence R description 735 source MCSA : MCSA1 59) chain A residue 74-94 type TRANSMEM sequence VLNAIVFTQLFAQAIMVYLPA description Helical source Swiss-Prot : SWS_FT_FI1 60) chain A residue 105-125 type TRANSMEM sequence LMWLSWWMAFIGLVVAALPLL description Helical source Swiss-Prot : SWS_FT_FI1 61) chain A residue 144-164 type TRANSMEM sequence AFYLGASVFVLSTWVSIYIVL description Helical source Swiss-Prot : SWS_FT_FI1 62) chain A residue 187-207 type TRANSMEM sequence VVFWLMWFLASLGLVLEAVLF description Helical source Swiss-Prot : SWS_FT_FI1 63) chain A residue 227-247 type TRANSMEM sequence LFWWTGHPIVYFWLLPAYAII description Helical source Swiss-Prot : SWS_FT_FI1 64) chain A residue 267-287 type TRANSMEM sequence LAFLLFLLLSTPVGFHHQFAD description Helical source Swiss-Prot : SWS_FT_FI1 65) chain A residue 300-320 type TRANSMEM sequence VLTLFVAVPSLMTAFTVAASL description Helical source Swiss-Prot : SWS_FT_FI1 66) chain A residue 345-365 type TRANSMEM sequence AFVAPVLGLLGFIPGGAGGIV description Helical source Swiss-Prot : SWS_FT_FI1 67) chain A residue 385-405 type TRANSMEM sequence FHLQVASLVTLTAMGSLYWLL description Helical source Swiss-Prot : SWS_FT_FI1 68) chain A residue 420-440 type TRANSMEM sequence LGLAVVWLWFLGMMIMAVGLH description Helical source Swiss-Prot : SWS_FT_FI1 69) chain A residue 471-491 type TRANSMEM sequence VLAGIVLLVALLLFIYGLFSV description Helical source Swiss-Prot : SWS_FT_FI1 70) chain A residue 527-547 type TRANSMEM sequence IGFWFAVAAILVVLAYGPTLV description Helical source Swiss-Prot : SWS_FT_FI1 71) chain A residue 237 type TOPO_DOM sequence Y description Periplasmic source Swiss-Prot : SWS_FT_FI3

Display surface Download Links