eF-site ID 5syh-AB PDB Code 5syh Chain A, B click to enlarge Title Structure of D141A variant of B. pseudomallei KatG Classification OXIDOREDUCTASE Compound Catalase-peroxidase Source (KATG_BURP1) Sequence A:  GTSNRDWWPNQLDLSILHRHSSLSDPMGKDFNYAQAFEKL DLAAVKRDLHALMTTSQDWWPADFGHYGGLFIRMAXHSAG TYRTADGRGGAGEGQQRFAPLNSWPANANLDKARRLLWPI KQKYGRAISWADLLILTGNVALESMGFKTFGFAGGRADTW EPEDVYWGSEKIWLELSGGPNSRYSGDRQLENPLAAVQMG LIYVNPEGPDGNPDPVAAARDIRDTFARMAMNDEETVALI AGGHTFGKTHGAGPASNVGAEPEAAGIEAQGLGWKSAYRT GKGADAITSGLEVTWTTTPTQWSHNFFENLFGYEWELTKS PAGAHQWVAKGADAVIPDAFDPSKKHRPTMLTTDLSLRFD PAYEKISRRFHENPEQFADAFARAWFKLTHRDMGPRARYL GPEVPAEVLLWQDPIPAVDHPLIDAADAAELKAKVLASGL TVSQLVSTAWAAASTFRGSDKRGGANGARIRLAPQKDWEA NQPEQLAAVLETLEAIRTAFNGAQRGGKQVSLADLIVLAG CAGVEQAAKNAGHAVTVPFAPGRADASQEQTDVESMAVLE PVADGFRNYLKGKYRVPAEVLLVDKAQLLTLSAPEMTVLL GGLRVLGANVGQSRHGVFTAREQALTNDFFVNLLDMGTEW KPTAADADVFEGRDRATGELKWTGTRVDLVFGSHSQLRAL AEVYGSADAQEKFVRDFVAVWNKVMNLDRFDLA B:  GTSNRDWWPNQLDLSILHRHSSLSDPMGKDFNYAQAFEKL DLAAVKRDLHALMTTSQDWWPADFGHYGGLFIRMAXHSAG TYRTADGRGGAGEGQQRFAPLNSWPANANLDKARRLLWPI KQKYGRAISWADLLILTGNVALESMGFKTFGFAGGRADTW EPEDVYWGSEKIWLELSGGPNSRYSGDRQLENPLAAVQMG LIYVNPEGPDGNPDPVAAARDIRDTFARMAMNDEETVALI AGGHTFGKTHGAGPASNVGAEPEAAGIEAQGLGWKSAYRT GKGADAITSGLEVTWTTTPTQWSHNFFENLFGYEWELTKS PAGAHQWVAKGADAVIPDAFDPSKKHRPTMLTTDLSLRFD PAYEKISRRFHENPEQFADAFARAWFKLTHRDMGPRARYL GPEVPAEVLLWQDPIPAVDHPLIDAADAAELKAKVLASGL TVSQLVSTAWAAASTFRGSDKRGGANGARIRLAPQKDWEA NQPEQLAAVLETLEAIRTAFNGAQRGGKQVSLADLIVLAG CAGVEQAAKNAGHAVTVPFAPGRADASQEQTDVESMAVLE PVADGFRNYLKGKYRVPAEVLLVDKAQLLTLSAPEMTVLL GGLRVLGANVGQSRHGVFTAREQALTNDFFVNLLDMGTEW KPTAADADVFEGRDRATGELKWTGTRVDLVFGSHSQLRAL AEVYGSADAQEKFVRDFVAVWNKVMNLDRFDLA Description Functional site 1) chain A residue 104 type sequence G description binding site for residue HEM A 801 source : AC1 2) chain A residue 105 type sequence L description binding site for residue HEM A 801 source : AC1 3) chain A residue 111 type sequence X description binding site for residue HEM A 801 source : AC1 4) chain A residue 241 type sequence P description binding site for residue HEM A 801 source : AC1 5) chain A residue 274 type sequence L description binding site for residue HEM A 801 source : AC1 6) chain A residue 275 type sequence I description binding site for residue HEM A 801 source : AC1 7) chain A residue 278 type sequence G description binding site for residue HEM A 801 source : AC1 8) chain A residue 279 type sequence H description binding site for residue HEM A 801 source : AC1 9) chain A residue 282 type sequence G description binding site for residue HEM A 801 source : AC1 10) chain A residue 283 type sequence K description binding site for residue HEM A 801 source : AC1 11) chain A residue 284 type sequence T description binding site for residue HEM A 801 source : AC1 12) chain A residue 285 type sequence H description binding site for residue HEM A 801 source : AC1 13) chain A residue 323 type sequence T description binding site for residue HEM A 801 source : AC1 14) chain A residue 324 type sequence S description binding site for residue HEM A 801 source : AC1 15) chain A residue 420 type sequence W description binding site for residue HEM A 801 source : AC1 16) chain A residue 122 type sequence G description binding site for residue NA A 802 source : AC2 17) chain A residue 123 type sequence R description binding site for residue NA A 802 source : AC2 18) chain A residue 124 type sequence G description binding site for residue NA A 802 source : AC2 19) chain A residue 494 type sequence S description binding site for residue NA A 802 source : AC2 20) chain A residue 124 type sequence G description binding site for residue CL A 803 source : AC3 21) chain A residue 198 type sequence E description binding site for residue CL A 803 source : AC3 22) chain A residue 200 type sequence V description binding site for residue CL A 803 source : AC3 23) chain A residue 108 type sequence R description binding site for residue OXY A 804 source : AC4 24) chain A residue 112 type sequence H description binding site for residue OXY A 804 source : AC4 25) chain A residue 141 type sequence A description binding site for residue OXY A 804 source : AC4 26) chain A residue 154 type sequence P description binding site for residue MPD A 805 source : AC5 27) chain A residue 323 type sequence T description binding site for residue MPD A 806 source : AC6 28) chain A residue 381 type sequence H description binding site for residue PO4 A 807 source : AC7 29) chain A residue 382 type sequence R description binding site for residue PO4 A 807 source : AC7 30) chain B residue 104 type sequence G description binding site for residue HEM B 801 source : AC8 31) chain B residue 105 type sequence L description binding site for residue HEM B 801 source : AC8 32) chain B residue 111 type sequence X description binding site for residue HEM B 801 source : AC8 33) chain B residue 239 type sequence V description binding site for residue HEM B 801 source : AC8 34) chain B residue 241 type sequence P description binding site for residue HEM B 801 source : AC8 35) chain B residue 274 type sequence L description binding site for residue HEM B 801 source : AC8 36) chain B residue 275 type sequence I description binding site for residue HEM B 801 source : AC8 37) chain B residue 278 type sequence G description binding site for residue HEM B 801 source : AC8 38) chain B residue 279 type sequence H description binding site for residue HEM B 801 source : AC8 39) chain B residue 282 type sequence G description binding site for residue HEM B 801 source : AC8 40) chain B residue 283 type sequence K description binding site for residue HEM B 801 source : AC8 41) chain B residue 284 type sequence T description binding site for residue HEM B 801 source : AC8 42) chain B residue 285 type sequence H description binding site for residue HEM B 801 source : AC8 43) chain B residue 323 type sequence T description binding site for residue HEM B 801 source : AC8 44) chain B residue 324 type sequence S description binding site for residue HEM B 801 source : AC8 45) chain B residue 388 type sequence T description binding site for residue HEM B 801 source : AC8 46) chain B residue 420 type sequence W description binding site for residue HEM B 801 source : AC8 47) chain B residue 122 type sequence G description binding site for residue NA B 802 source : AC9 48) chain B residue 123 type sequence R description binding site for residue NA B 802 source : AC9 49) chain B residue 124 type sequence G description binding site for residue NA B 802 source : AC9 50) chain B residue 494 type sequence S description binding site for residue NA B 802 source : AC9 51) chain B residue 124 type sequence G description binding site for residue CL B 803 source : AD1 52) chain B residue 198 type sequence E description binding site for residue CL B 803 source : AD1 53) chain B residue 200 type sequence V description binding site for residue CL B 803 source : AD1 54) chain B residue 108 type sequence R description binding site for residue OXY B 804 source : AD2 55) chain B residue 112 type sequence H description binding site for residue OXY B 804 source : AD2 56) chain B residue 141 type sequence A description binding site for residue OXY B 804 source : AD2 57) chain B residue 323 type sequence T description binding site for residue MPD B 805 source : AD3 58) chain B residue 324 type sequence S description binding site for residue MPD B 805 source : AD3 59) chain B residue 380 type sequence K description binding site for residue PO4 B 807 source : AD5 60) chain B residue 381 type sequence H description binding site for residue PO4 B 807 source : AD5 61) chain B residue 382 type sequence R description binding site for residue PO4 B 807 source : AD5 62) chain A residue 271-281 type prosite sequence TVALIAGGHTF description PEROXIDASE_1 Peroxidases proximal heme-ligand signature. TVALIAGGHTF source prosite : PS00435 63) chain A residue 112 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01961 source Swiss-Prot : SWS_FT_FI1 64) chain B residue 112 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01961 source Swiss-Prot : SWS_FT_FI1 65) chain A residue 279 type BINDING sequence H description axial binding residue => ECO:0000255|HAMAP-Rule:MF_01961 source Swiss-Prot : SWS_FT_FI2 66) chain B residue 279 type BINDING sequence H description axial binding residue => ECO:0000255|HAMAP-Rule:MF_01961 source Swiss-Prot : SWS_FT_FI2 67) chain A residue 108 type SITE sequence R description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01961 source Swiss-Prot : SWS_FT_FI3 68) chain B residue 108 type SITE sequence R description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01961 source Swiss-Prot : SWS_FT_FI3 69) chain A residue 111 type CROSSLNK sequence X description Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244) => ECO:0000255|HAMAP-Rule:MF_01961 source Swiss-Prot : SWS_FT_FI4 70) chain B residue 111 type CROSSLNK sequence X description Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244) => ECO:0000255|HAMAP-Rule:MF_01961 source Swiss-Prot : SWS_FT_FI4 71) chain B residue 238 type CROSSLNK sequence Y description Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) => ECO:0000255|HAMAP-Rule:MF_01961 source Swiss-Prot : SWS_FT_FI5 72) chain B residue 264 type CROSSLNK sequence M description Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) => ECO:0000255|HAMAP-Rule:MF_01961 source Swiss-Prot : SWS_FT_FI5 73) chain A residue 238 type CROSSLNK sequence Y description Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) => ECO:0000255|HAMAP-Rule:MF_01961 source Swiss-Prot : SWS_FT_FI5 74) chain A residue 264 type CROSSLNK sequence M description Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) => ECO:0000255|HAMAP-Rule:MF_01961 source Swiss-Prot : SWS_FT_FI5

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