eF-site ID 3a2w-ABCDEFGHIJ PDB Code 3a2w Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title Peroxiredoxin (C50S) from Aeropytum pernix K1 (peroxide-bound form) Classification OXIDOREDUCTASE Compound Probable peroxiredoxin Source Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) (TDXH_AERPE) Sequence A:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS HPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL YEEA B:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS HPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL YEEA C:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS HPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL YEE D:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS HPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL YEEA E:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS HPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL YEE F:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS HPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL YEEA G:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS HPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL YEE H:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS HPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL YEEA I:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS HPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL YEEA J:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS HPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL YEEA Description Functional site 1) chain A residue 43 type sequence P description BINDING SITE FOR RESIDUE GOL A 251 source : AC1 2) chain A residue 47 type sequence T description BINDING SITE FOR RESIDUE GOL A 251 source : AC1 3) chain A residue 48 type sequence P description BINDING SITE FOR RESIDUE GOL A 251 source : AC1 4) chain A residue 49 type sequence V description BINDING SITE FOR RESIDUE GOL A 251 source : AC1 5) chain A residue 50 type sequence S description BINDING SITE FOR RESIDUE GOL A 251 source : AC1 6) chain A residue 126 type sequence R description BINDING SITE FOR RESIDUE GOL A 251 source : AC1 7) chain B residue 189 type sequence P description BINDING SITE FOR RESIDUE GOL A 251 source : AC1 8) chain B residue 47 type sequence T description BINDING SITE FOR RESIDUE PER B 1 source : AC2 9) chain B residue 48 type sequence P description BINDING SITE FOR RESIDUE PER B 1 source : AC2 10) chain B residue 49 type sequence V description BINDING SITE FOR RESIDUE PER B 1 source : AC2 11) chain B residue 50 type sequence S description BINDING SITE FOR RESIDUE PER B 1 source : AC2 12) chain B residue 126 type sequence R description BINDING SITE FOR RESIDUE PER B 1 source : AC2 13) chain C residue 47 type sequence T description BINDING SITE FOR RESIDUE GOL C 251 source : AC3 14) chain C residue 48 type sequence P description BINDING SITE FOR RESIDUE GOL C 251 source : AC3 15) chain C residue 49 type sequence V description BINDING SITE FOR RESIDUE GOL C 251 source : AC3 16) chain C residue 50 type sequence S description BINDING SITE FOR RESIDUE GOL C 251 source : AC3 17) chain C residue 126 type sequence R description BINDING SITE FOR RESIDUE GOL C 251 source : AC3 18) chain D residue 47 type sequence T description BINDING SITE FOR RESIDUE GOL D 251 source : AC4 19) chain D residue 48 type sequence P description BINDING SITE FOR RESIDUE GOL D 251 source : AC4 20) chain D residue 49 type sequence V description BINDING SITE FOR RESIDUE GOL D 251 source : AC4 21) chain D residue 50 type sequence S description BINDING SITE FOR RESIDUE GOL D 251 source : AC4 22) chain D residue 126 type sequence R description BINDING SITE FOR RESIDUE GOL D 251 source : AC4 23) chain E residue 47 type sequence T description BINDING SITE FOR RESIDUE GOL E 251 source : AC5 24) chain E residue 48 type sequence P description BINDING SITE FOR RESIDUE GOL E 251 source : AC5 25) chain E residue 49 type sequence V description BINDING SITE FOR RESIDUE GOL E 251 source : AC5 26) chain E residue 50 type sequence S description BINDING SITE FOR RESIDUE GOL E 251 source : AC5 27) chain E residue 126 type sequence R description BINDING SITE FOR RESIDUE GOL E 251 source : AC5 28) chain F residue 47 type sequence T description BINDING SITE FOR RESIDUE PER F 251 source : AC6 29) chain F residue 48 type sequence P description BINDING SITE FOR RESIDUE PER F 251 source : AC6 30) chain F residue 49 type sequence V description BINDING SITE FOR RESIDUE PER F 251 source : AC6 31) chain F residue 50 type sequence S description BINDING SITE FOR RESIDUE PER F 251 source : AC6 32) chain F residue 126 type sequence R description BINDING SITE FOR RESIDUE PER F 251 source : AC6 33) chain G residue 47 type sequence T description BINDING SITE FOR RESIDUE GOL G 251 source : AC7 34) chain G residue 48 type sequence P description BINDING SITE FOR RESIDUE GOL G 251 source : AC7 35) chain G residue 49 type sequence V description BINDING SITE FOR RESIDUE GOL G 251 source : AC7 36) chain G residue 50 type sequence S description BINDING SITE FOR RESIDUE GOL G 251 source : AC7 37) chain G residue 126 type sequence R description BINDING SITE FOR RESIDUE GOL G 251 source : AC7 38) chain G residue 145 type sequence M description BINDING SITE FOR RESIDUE GOL G 251 source : AC7 39) chain H residue 47 type sequence T description BINDING SITE FOR RESIDUE GOL H 251 source : AC8 40) chain H residue 48 type sequence P description BINDING SITE FOR RESIDUE GOL H 251 source : AC8 41) chain H residue 49 type sequence V description BINDING SITE FOR RESIDUE GOL H 251 source : AC8 42) chain H residue 50 type sequence S description BINDING SITE FOR RESIDUE GOL H 251 source : AC8 43) chain H residue 126 type sequence R description BINDING SITE FOR RESIDUE GOL H 251 source : AC8 44) chain I residue 47 type sequence T description BINDING SITE FOR RESIDUE PER I 251 source : AC9 45) chain I residue 48 type sequence P description BINDING SITE FOR RESIDUE PER I 251 source : AC9 46) chain I residue 49 type sequence V description BINDING SITE FOR RESIDUE PER I 251 source : AC9 47) chain I residue 50 type sequence S description BINDING SITE FOR RESIDUE PER I 251 source : AC9 48) chain I residue 126 type sequence R description BINDING SITE FOR RESIDUE PER I 251 source : AC9 49) chain J residue 47 type sequence T description BINDING SITE FOR RESIDUE GOL J 1 source : BC1 50) chain J residue 48 type sequence P description BINDING SITE FOR RESIDUE GOL J 1 source : BC1 51) chain J residue 49 type sequence V description BINDING SITE FOR RESIDUE GOL J 1 source : BC1 52) chain J residue 50 type sequence S description BINDING SITE FOR RESIDUE GOL J 1 source : BC1 53) chain J residue 126 type sequence R description BINDING SITE FOR RESIDUE GOL J 1 source : BC1 54) chain A residue 126 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903 source Swiss-Prot : SWS_FT_FI2 55) chain J residue 126 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903 source Swiss-Prot : SWS_FT_FI2 56) chain B residue 126 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903 source Swiss-Prot : SWS_FT_FI2 57) chain C residue 126 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903 source Swiss-Prot : SWS_FT_FI2 58) chain D residue 126 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903 source Swiss-Prot : SWS_FT_FI2 59) chain E residue 126 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903 source Swiss-Prot : SWS_FT_FI2 60) chain F residue 126 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903 source Swiss-Prot : SWS_FT_FI2 61) chain G residue 126 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903 source Swiss-Prot : SWS_FT_FI2 62) chain H residue 126 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903 source Swiss-Prot : SWS_FT_FI2 63) chain I residue 126 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903 source Swiss-Prot : SWS_FT_FI2 64) chain A residue 50 type ACT_SITE sequence S description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649 source Swiss-Prot : SWS_FT_FI1 65) chain J residue 50 type ACT_SITE sequence S description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649 source Swiss-Prot : SWS_FT_FI1 66) chain B residue 50 type ACT_SITE sequence S description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649 source Swiss-Prot : SWS_FT_FI1 67) chain C residue 50 type ACT_SITE sequence S description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649 source Swiss-Prot : SWS_FT_FI1 68) chain D residue 50 type ACT_SITE sequence S description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649 source Swiss-Prot : SWS_FT_FI1 69) chain E residue 50 type ACT_SITE sequence S description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649 source Swiss-Prot : SWS_FT_FI1 70) chain F residue 50 type ACT_SITE sequence S description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649 source Swiss-Prot : SWS_FT_FI1 71) chain G residue 50 type ACT_SITE sequence S description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649 source Swiss-Prot : SWS_FT_FI1 72) chain H residue 50 type ACT_SITE sequence S description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649 source Swiss-Prot : SWS_FT_FI1 73) chain I residue 50 type ACT_SITE sequence S description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649 source Swiss-Prot : SWS_FT_FI1

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