eF-site ID 4enp-ABCD PDB Code 4enp Chain A, B, C, D Title Structure of E530A variant E. coli KatE Classification OXIDOREDUCTASE Compound Catalase HPII Source Escherichia coli (strain K12) (CATE_ECOLI) Sequence A:  SLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLNS LEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLED FILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDI TKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFAT KFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHW AIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYR TMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDEA QKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDEF KFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENE QAAFHPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGPN FHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSIND NWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYSH PRLFWLSQTPFEQRHIVDGFSFALSKVVRPYIRERVVDQL AHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDPS LSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAKG VHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVIV PCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKAT IKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIPK IDKIPA B:  SLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLNS LEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLED FILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDI TKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFAT KFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHW AIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYR TMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDEA QKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDEF KFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENE QAAFHPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGPN FHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSIND NWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYSH PRLFWLSQTPFEQRHIVDGFSFALSKVVRPYIRERVVDQL AHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDPS LSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAKG VHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVIV PCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKAT IKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIPK IDKIPA C:  SLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLNS LEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLED FILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDI TKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFAT KFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHW AIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYR TMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDEA QKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDEF KFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENE QAAFHPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGPN FHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSIND NWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYSH PRLFWLSQTPFEQRHIVDGFSFALSKVVRPYIRERVVDQL AHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDPS LSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAKG VHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVIV PCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKAT IKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIPK IDKIPA D:  SLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLNS LEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLED FILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDI TKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFAT KFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHW AIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYR TMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDEA QKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDEF KFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENE QAAFHPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGPN FHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSIND NWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYSH PRLFWLSQTPFEQRHIVDGFSFALSKVVRPYIRERVVDQL AHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDPS LSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAKG VHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVIV PCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKAT IKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIPK IDKIPA Description Functional site 1) chain A residue 125 type sequence R description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 2) chain A residue 126 type sequence I description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 3) chain A residue 127 type sequence V description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 4) chain A residue 128 type sequence H description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 5) chain A residue 165 type sequence R description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 6) chain A residue 184 type sequence G description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 7) chain A residue 199 type sequence V description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 8) chain A residue 200 type sequence G description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 9) chain A residue 201 type sequence N description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 10) chain A residue 214 type sequence F description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 11) chain A residue 275 type sequence H description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 12) chain A residue 391 type sequence F description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 13) chain A residue 407 type sequence L description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 14) chain A residue 411 type sequence R description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 15) chain A residue 414 type sequence S description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 16) chain A residue 415 type sequence Y description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 17) chain A residue 418 type sequence T description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 18) chain A residue 419 type sequence Q description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 19) chain A residue 422 type sequence R description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 20) chain D residue 118 type sequence D description BINDING SITE FOR RESIDUE HEM A 801 source : AC1 21) chain B residue 125 type sequence R description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 22) chain B residue 126 type sequence I description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 23) chain B residue 127 type sequence V description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 24) chain B residue 128 type sequence H description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 25) chain B residue 165 type sequence R description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 26) chain B residue 184 type sequence G description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 27) chain B residue 199 type sequence V description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 28) chain B residue 200 type sequence G description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 29) chain B residue 201 type sequence N description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 30) chain B residue 206 type sequence F description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 31) chain B residue 214 type sequence F description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 32) chain B residue 274 type sequence I description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 33) chain B residue 275 type sequence H description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 34) chain B residue 391 type sequence F description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 35) chain B residue 407 type sequence L description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 36) chain B residue 411 type sequence R description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 37) chain B residue 414 type sequence S description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 38) chain B residue 415 type sequence Y description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 39) chain B residue 418 type sequence T description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 40) chain B residue 419 type sequence Q description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 41) chain B residue 422 type sequence R description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 42) chain C residue 118 type sequence D description BINDING SITE FOR RESIDUE HEM B 801 source : AC2 43) chain B residue 118 type sequence D description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 44) chain C residue 125 type sequence R description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 45) chain C residue 126 type sequence I description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 46) chain C residue 127 type sequence V description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 47) chain C residue 128 type sequence H description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 48) chain C residue 165 type sequence R description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 49) chain C residue 184 type sequence G description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 50) chain C residue 199 type sequence V description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 51) chain C residue 200 type sequence G description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 52) chain C residue 201 type sequence N description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 53) chain C residue 206 type sequence F description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 54) chain C residue 214 type sequence F description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 55) chain C residue 274 type sequence I description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 56) chain C residue 275 type sequence H description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 57) chain C residue 391 type sequence F description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 58) chain C residue 407 type sequence L description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 59) chain C residue 411 type sequence R description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 60) chain C residue 414 type sequence S description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 61) chain C residue 415 type sequence Y description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 62) chain C residue 418 type sequence T description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 63) chain C residue 419 type sequence Q description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 64) chain C residue 422 type sequence R description BINDING SITE FOR RESIDUE HEM C 801 source : AC3 65) chain D residue 125 type sequence R description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 66) chain D residue 126 type sequence I description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 67) chain D residue 127 type sequence V description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 68) chain D residue 128 type sequence H description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 69) chain D residue 165 type sequence R description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 70) chain D residue 184 type sequence G description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 71) chain D residue 199 type sequence V description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 72) chain D residue 200 type sequence G description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 73) chain D residue 201 type sequence N description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 74) chain D residue 206 type sequence F description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 75) chain D residue 214 type sequence F description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 76) chain D residue 275 type sequence H description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 77) chain D residue 391 type sequence F description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 78) chain D residue 407 type sequence L description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 79) chain D residue 411 type sequence R description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 80) chain D residue 414 type sequence S description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 81) chain D residue 415 type sequence Y description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 82) chain D residue 418 type sequence T description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 83) chain D residue 419 type sequence Q description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 84) chain D residue 422 type sequence R description BINDING SITE FOR RESIDUE HEM D 801 source : AC4 85) chain A residue 128 type catalytic sequence H description 573 source MCSA : MCSA1 86) chain A residue 201 type catalytic sequence N description 573 source MCSA : MCSA1 87) chain A residue 392 type catalytic sequence H description 573 source MCSA : MCSA1 88) chain B residue 128 type catalytic sequence H description 573 source MCSA : MCSA2 89) chain B residue 201 type catalytic sequence N description 573 source MCSA : MCSA2 90) chain B residue 392 type catalytic sequence H description 573 source MCSA : MCSA2 91) chain C residue 128 type catalytic sequence H description 573 source MCSA : MCSA3 92) chain C residue 201 type catalytic sequence N description 573 source MCSA : MCSA3 93) chain C residue 392 type catalytic sequence H description 573 source MCSA : MCSA3 94) chain D residue 128 type catalytic sequence H description 573 source MCSA : MCSA4 95) chain D residue 201 type catalytic sequence N description 573 source MCSA : MCSA4 96) chain D residue 392 type catalytic sequence H description 573 source MCSA : MCSA4 97) chain A residue 392 type CROSSLNK sequence H description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 98) chain A residue 415 type CROSSLNK sequence Y description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 99) chain B residue 392 type CROSSLNK sequence H description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 100) chain B residue 415 type CROSSLNK sequence Y description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 101) chain C residue 392 type CROSSLNK sequence H description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 102) chain C residue 415 type CROSSLNK sequence Y description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 103) chain D residue 392 type CROSSLNK sequence H description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 104) chain D residue 415 type CROSSLNK sequence Y description 3'-histidyl-3-tyrosine (His-Tyr) source Swiss-Prot : SWS_FT_FI3 105) chain A residue 128 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 106) chain A residue 201 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 107) chain B residue 128 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 108) chain B residue 201 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 109) chain C residue 128 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 110) chain C residue 201 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 111) chain D residue 128 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 112) chain D residue 201 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 source Swiss-Prot : SWS_FT_FI1 113) chain A residue 415 type BINDING sequence Y description axial binding residue source Swiss-Prot : SWS_FT_FI2 114) chain B residue 415 type BINDING sequence Y description axial binding residue source Swiss-Prot : SWS_FT_FI2 115) chain C residue 415 type BINDING sequence Y description axial binding residue source Swiss-Prot : SWS_FT_FI2 116) chain D residue 415 type BINDING sequence Y description axial binding residue source Swiss-Prot : SWS_FT_FI2 117) chain A residue 411-419 type prosite sequence RLFSYTDTQ description CATALASE_1 Catalase proximal heme-ligand signature. RLFSYtDTQ source prosite : PS00437 118) chain A residue 117-133 type prosite sequence FDHERIPERIVHARGSA description CATALASE_2 Catalase proximal active site signature. FdHeripERivHarGSA source prosite : PS00438

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