eF-site ID 1qf7-ABCD PDB Code 1qf7 Chain A, B, C, D Title STRUCTURE OF THE MUTANT HIS392GLN OF CATALASE HPII FROM E. COLI Classification OXIDOREDUCTASE Compound PROTEIN (CATALASE HPII) Source (CATE_ECOLI) Sequence A:  DSLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLN SLEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLE DFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSD ITKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFA TKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPH WAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSY RTMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDE AQKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDE FKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAEN EQAAFQPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGP NFHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSIN DNWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYS HPRLFWLSQTPFEQRHIVDGFSFELSKVVRPYIRERVVDQ LAHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDP SLSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAK GVHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVI VPCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKA TIKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIP KIDKIPA B:  DSLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLN SLEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLE DFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSD ITKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFA TKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPH WAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSY RTMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDE AQKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDE FKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAEN EQAAFQPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGP NFHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSIN DNWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYS HPRLFWLSQTPFEQRHIVDGFSFELSKVVRPYIRERVVDQ LAHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDP SLSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAK GVHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVI VPCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKA TIKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIP KIDKIPA C:  DSLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLN SLEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLE DFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSD ITKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFA TKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPH WAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSY RTMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDE AQKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDE FKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAEN EQAAFQPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGP NFHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSIN DNWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYS HPRLFWLSQTPFEQRHIVDGFSFELSKVVRPYIRERVVDQ LAHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDP SLSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAK GVHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVI VPCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKA TIKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIP KIDKIPA D:  DSLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLN SLEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLE DFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSD ITKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFA TKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPH WAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSY RTMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDE AQKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDE FKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAEN EQAAFQPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGP NFHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSIN DNWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYS HPRLFWLSQTPFEQRHIVDGFSFELSKVVRPYIRERVVDQ LAHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDP SLSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAK GVHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVI VPCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKA TIKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIP KIDKIPA Description Functional site 1) chain A residue 128 type sequence H description ESSENTIAL CATALYTIC RESIDUES. source : CAA 2) chain A residue 201 type sequence N description ESSENTIAL CATALYTIC RESIDUES. source : CAA 3) chain A residue 415 type sequence Y description ESSENTIAL CATALYTIC RESIDUES. source : CAA 4) chain B residue 128 type sequence H description ESSENTIAL CATALYTIC RESIDUES. source : CAB 5) chain B residue 201 type sequence N description ESSENTIAL CATALYTIC RESIDUES. source : CAB 6) chain B residue 415 type sequence Y description ESSENTIAL CATALYTIC RESIDUES. source : CAB 7) chain C residue 128 type sequence H description ESSENTIAL CATALYTIC RESIDUES. source : CAC 8) chain C residue 201 type sequence N description ESSENTIAL CATALYTIC RESIDUES. source : CAC 9) chain C residue 415 type sequence Y description ESSENTIAL CATALYTIC RESIDUES. source : CAC 10) chain D residue 128 type sequence H description ESSENTIAL CATALYTIC RESIDUES. source : CAD 11) chain D residue 201 type sequence N description ESSENTIAL CATALYTIC RESIDUES. source : CAD 12) chain D residue 415 type sequence Y description ESSENTIAL CATALYTIC RESIDUES. source : CAD 13) chain A residue 125 type sequence R description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 14) chain A residue 126 type sequence I description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 15) chain A residue 127 type sequence V description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 16) chain A residue 128 type sequence H description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 17) chain A residue 165 type sequence R description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 18) chain A residue 184 type sequence G description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 19) chain A residue 199 type sequence V description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 20) chain A residue 200 type sequence G description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 21) chain A residue 201 type sequence N description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 22) chain A residue 214 type sequence F description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 23) chain A residue 274 type sequence I description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 24) chain A residue 275 type sequence H description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 25) chain A residue 391 type sequence F description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 26) chain A residue 407 type sequence L description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 27) chain A residue 411 type sequence R description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 28) chain A residue 414 type sequence S description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 29) chain A residue 415 type sequence Y description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 30) chain A residue 418 type sequence T description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 31) chain A residue 419 type sequence Q description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 32) chain A residue 422 type sequence R description BINDING SITE FOR RESIDUE HEM A 754 source : AC1 33) chain B residue 125 type sequence R description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 34) chain B residue 126 type sequence I description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 35) chain B residue 127 type sequence V description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 36) chain B residue 128 type sequence H description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 37) chain B residue 165 type sequence R description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 38) chain B residue 184 type sequence G description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 39) chain B residue 199 type sequence V description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 40) chain B residue 200 type sequence G description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 41) chain B residue 201 type sequence N description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 42) chain B residue 206 type sequence F description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 43) chain B residue 214 type sequence F description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 44) chain B residue 274 type sequence I description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 45) chain B residue 275 type sequence H description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 46) chain B residue 391 type sequence F description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 47) chain B residue 407 type sequence L description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 48) chain B residue 411 type sequence R description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 49) chain B residue 414 type sequence S description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 50) chain B residue 415 type sequence Y description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 51) chain B residue 418 type sequence T description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 52) chain B residue 419 type sequence Q description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 53) chain B residue 422 type sequence R description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 54) chain C residue 118 type sequence D description BINDING SITE FOR RESIDUE HEM B 754 source : AC2 55) chain C residue 125 type sequence R description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 56) chain C residue 126 type sequence I description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 57) chain C residue 127 type sequence V description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 58) chain C residue 128 type sequence H description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 59) chain C residue 165 type sequence R description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 60) chain C residue 184 type sequence G description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 61) chain C residue 199 type sequence V description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 62) chain C residue 200 type sequence G description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 63) chain C residue 201 type sequence N description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 64) chain C residue 214 type sequence F description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 65) chain C residue 275 type sequence H description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 66) chain C residue 391 type sequence F description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 67) chain C residue 407 type sequence L description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 68) chain C residue 411 type sequence R description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 69) chain C residue 414 type sequence S description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 70) chain C residue 415 type sequence Y description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 71) chain C residue 418 type sequence T description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 72) chain C residue 419 type sequence Q description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 73) chain C residue 422 type sequence R description BINDING SITE FOR RESIDUE HEM C 754 source : AC3 74) chain A residue 118 type sequence D description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 75) chain D residue 125 type sequence R description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 76) chain D residue 126 type sequence I description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 77) chain D residue 127 type sequence V description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 78) chain D residue 128 type sequence H description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 79) chain D residue 165 type sequence R description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 80) chain D residue 184 type sequence G description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 81) chain D residue 199 type sequence V description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 82) chain D residue 200 type sequence G description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 83) chain D residue 201 type sequence N description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 84) chain D residue 214 type sequence F description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 85) chain D residue 274 type sequence I description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 86) chain D residue 275 type sequence H description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 87) chain D residue 391 type sequence F description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 88) chain D residue 407 type sequence L description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 89) chain D residue 411 type sequence R description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 90) chain D residue 414 type sequence S description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 91) chain D residue 415 type sequence Y description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 92) chain D residue 418 type sequence T description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 93) chain D residue 419 type sequence Q description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 94) chain D residue 422 type sequence R description BINDING SITE FOR RESIDUE HEM D 754 source : AC4 95) chain A residue 128 type catalytic sequence H description 573 source MCSA : MCSA1 96) chain A residue 201 type catalytic sequence N description 573 source MCSA : MCSA1 97) chain A residue 392 type catalytic sequence Q description 573 source MCSA : MCSA1 98) chain B residue 128 type catalytic sequence H description 573 source MCSA : MCSA2 99) chain B residue 201 type catalytic sequence N description 573 source MCSA : MCSA2 100) chain B residue 392 type catalytic sequence Q description 573 source MCSA : MCSA2 101) chain C residue 128 type catalytic sequence H description 573 source MCSA : MCSA3 102) chain C residue 201 type catalytic sequence N description 573 source MCSA : MCSA3 103) chain C residue 392 type catalytic sequence Q description 573 source MCSA : MCSA3 104) chain D residue 128 type catalytic sequence H description 573 source MCSA : MCSA4 105) chain D residue 201 type catalytic sequence N description 573 source MCSA : MCSA4 106) chain D residue 392 type catalytic sequence Q description 573 source MCSA : MCSA4 107) chain A residue 411-419 type prosite sequence RLFSYTDTQ description CATALASE_1 Catalase proximal heme-ligand signature. RLFSYtDTQ source prosite : PS00437 108) chain A residue 117-133 type prosite sequence FDHERIPERIVHARGSA description CATALASE_2 Catalase proximal active site signature. FdHeripERivHarGSA source prosite : PS00438 109) chain A residue 128 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 110) chain A residue 201 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 111) chain B residue 128 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 112) chain B residue 201 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 113) chain C residue 128 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 114) chain C residue 201 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 115) chain D residue 128 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 116) chain D residue 201 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 117) chain A residue 415 type BINDING sequence Y description axial binding residue source Swiss-Prot : SWS_FT_FI2 118) chain B residue 415 type BINDING sequence Y description axial binding residue source Swiss-Prot : SWS_FT_FI2 119) chain C residue 415 type BINDING sequence Y description axial binding residue source Swiss-Prot : SWS_FT_FI2 120) chain D residue 415 type BINDING sequence Y description axial binding residue source Swiss-Prot : SWS_FT_FI2 121) chain A residue 392 type CROSSLNK sequence Q description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 122) chain A residue 415 type CROSSLNK sequence Y description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 123) chain B residue 392 type CROSSLNK sequence Q description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 124) chain B residue 415 type CROSSLNK sequence Y description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 125) chain C residue 392 type CROSSLNK sequence Q description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 126) chain C residue 415 type CROSSLNK sequence Y description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 127) chain D residue 392 type CROSSLNK sequence Q description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 128) chain D residue 415 type CROSSLNK sequence Y description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3

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