eF-site ID 2fch-ABCDEFG PDB Code 2fch Chain A, B, C, D, E, F, G click to enlarge Title Crystal Structure of Thioredoxin Mutant G74S Classification ELECTRON TRANSPORT Compound Thioredoxin 1 Source Escherichia coli (strain K12) (THIO_ECOLI) Sequence A:  DKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPI LDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRSIPTLLLF KNGEVAATKVGALSKGQLKEFLDANL B:  DKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPI LDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRSIPTLLLF KNGEVAATKVGALSKGQLKEFLDANL C:  KIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPIL DEIADEYQGKLTVAKLNIDQNPGTAPKYGIRSIPTLLLFK NGEVAATKVGALSKGQLKEFLDANLA D:  DKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPI LDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRSIPTLLLF KNGEVAATKVGALSKGQLKEFLDANLA E:  DKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPI LDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRSIPTLLLF KNGEVAATKVGALSKGQLKEFLDANLA F:  DKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPI LDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRSIPTLLLF KNGEVAATKVGALSKGQLKEFLDANL G:  DKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPI LDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRSIPTLLLF KNGEVAATKVGALSKGQLKEFLDANLA Description Functional site 1) chain B residue 70 type sequence Y description BINDING SITE FOR RESIDUE MPD D 501 source : AC1 2) chain D residue 70 type sequence Y description BINDING SITE FOR RESIDUE MPD D 501 source : AC1 3) chain D residue 71 type sequence G description BINDING SITE FOR RESIDUE MPD D 501 source : AC1 4) chain D residue 89 type sequence T description BINDING SITE FOR RESIDUE MPD D 501 source : AC1 5) chain E residue 60 type sequence I description BINDING SITE FOR RESIDUE MPD E 502 source : AC2 6) chain E residue 67 type sequence A description BINDING SITE FOR RESIDUE MPD E 502 source : AC2 7) chain E residue 73 type sequence R description BINDING SITE FOR RESIDUE MPD E 502 source : AC2 8) chain E residue 74 type sequence S description BINDING SITE FOR RESIDUE MPD E 502 source : AC2 9) chain A residue 70 type sequence Y description BINDING SITE FOR RESIDUE MPD E 503 source : AC3 10) chain A residue 89 type sequence T description BINDING SITE FOR RESIDUE MPD E 503 source : AC3 11) chain E residue 70 type sequence Y description BINDING SITE FOR RESIDUE MPD E 503 source : AC3 12) chain E residue 71 type sequence G description BINDING SITE FOR RESIDUE MPD E 503 source : AC3 13) chain E residue 89 type sequence T description BINDING SITE FOR RESIDUE MPD E 503 source : AC3 14) chain F residue 31 type sequence W description BINDING SITE FOR RESIDUE MPD G 504 source : AC4 15) chain F residue 60 type sequence I description BINDING SITE FOR RESIDUE MPD G 504 source : AC4 16) chain F residue 72 type sequence I description BINDING SITE FOR RESIDUE MPD G 504 source : AC4 17) chain F residue 73 type sequence R description BINDING SITE FOR RESIDUE MPD G 504 source : AC4 18) chain F residue 74 type sequence S description BINDING SITE FOR RESIDUE MPD G 504 source : AC4 19) chain G residue 70 type sequence Y description BINDING SITE FOR RESIDUE MPD G 504 source : AC4 20) chain G residue 71 type sequence G description BINDING SITE FOR RESIDUE MPD G 504 source : AC4 21) chain B residue 73 type sequence R description BINDING SITE FOR RESIDUE MPD D 505 source : AC5 22) chain C residue 41 type sequence I description BINDING SITE FOR RESIDUE MPD D 505 source : AC5 23) chain C residue 44 type sequence E description BINDING SITE FOR RESIDUE MPD D 505 source : AC5 24) chain C residue 96 type sequence K description BINDING SITE FOR RESIDUE MPD D 505 source : AC5 25) chain D residue 70 type sequence Y description BINDING SITE FOR RESIDUE MPD D 505 source : AC5 26) chain D residue 84 type sequence G description BINDING SITE FOR RESIDUE MPD D 505 source : AC5 27) chain D residue 85 type sequence E description BINDING SITE FOR RESIDUE MPD D 505 source : AC5 28) chain D residue 86 type sequence V description BINDING SITE FOR RESIDUE MPD D 505 source : AC5 29) chain D residue 60 type sequence I description BINDING SITE FOR RESIDUE MPD D 506 source : AC6 30) chain D residue 72 type sequence I description BINDING SITE FOR RESIDUE MPD D 506 source : AC6 31) chain D residue 73 type sequence R description BINDING SITE FOR RESIDUE MPD D 506 source : AC6 32) chain E residue 36 type sequence K description BINDING SITE FOR RESIDUE MPD D 506 source : AC6 33) chain A residue 72 type sequence I description BINDING SITE FOR RESIDUE MPD A 507 source : AC7 34) chain B residue 36 type sequence K description BINDING SITE FOR RESIDUE MPD A 507 source : AC7 35) chain B residue 40 type sequence P description BINDING SITE FOR RESIDUE MPD A 507 source : AC7 36) chain A residue 24-42 type prosite sequence LVDFWAEWCGPCKMIAPIL description THIOREDOXIN_1 Thioredoxin family active site. LVdFWaeWCGPCKmIapiL source prosite : PS00194 37) chain A residue 33 type ACT_SITE sequence G description Nucleophile source Swiss-Prot : SWS_FT_FI1 38) chain E residue 36 type ACT_SITE sequence K description Nucleophile source Swiss-Prot : SWS_FT_FI1 39) chain F residue 33 type ACT_SITE sequence G description Nucleophile source Swiss-Prot : SWS_FT_FI1 40) chain F residue 36 type ACT_SITE sequence K description Nucleophile source Swiss-Prot : SWS_FT_FI1 41) chain G residue 33 type ACT_SITE sequence G description Nucleophile source Swiss-Prot : SWS_FT_FI1 42) chain G residue 36 type ACT_SITE sequence K description Nucleophile source Swiss-Prot : SWS_FT_FI1 43) chain A residue 36 type ACT_SITE sequence K description Nucleophile source Swiss-Prot : SWS_FT_FI1 44) chain B residue 33 type ACT_SITE sequence G description Nucleophile source Swiss-Prot : SWS_FT_FI1 45) chain B residue 36 type ACT_SITE sequence K description Nucleophile source Swiss-Prot : SWS_FT_FI1 46) chain C residue 33 type ACT_SITE sequence G description Nucleophile source Swiss-Prot : SWS_FT_FI1 47) chain C residue 36 type ACT_SITE sequence K description Nucleophile source Swiss-Prot : SWS_FT_FI1 48) chain D residue 33 type ACT_SITE sequence G description Nucleophile source Swiss-Prot : SWS_FT_FI1 49) chain D residue 36 type ACT_SITE sequence K description Nucleophile source Swiss-Prot : SWS_FT_FI1 50) chain E residue 33 type ACT_SITE sequence G description Nucleophile source Swiss-Prot : SWS_FT_FI1 51) chain A residue 27 type SITE sequence F description Deprotonates C-terminal active site Cys source Swiss-Prot : SWS_FT_FI2 52) chain B residue 27 type SITE sequence F description Deprotonates C-terminal active site Cys source Swiss-Prot : SWS_FT_FI2 53) chain C residue 27 type SITE sequence F description Deprotonates C-terminal active site Cys source Swiss-Prot : SWS_FT_FI2 54) chain D residue 27 type SITE sequence F description Deprotonates C-terminal active site Cys source Swiss-Prot : SWS_FT_FI2 55) chain E residue 27 type SITE sequence F description Deprotonates C-terminal active site Cys source Swiss-Prot : SWS_FT_FI2 56) chain F residue 27 type SITE sequence F description Deprotonates C-terminal active site Cys source Swiss-Prot : SWS_FT_FI2 57) chain G residue 27 type SITE sequence F description Deprotonates C-terminal active site Cys source Swiss-Prot : SWS_FT_FI2 58) chain A residue 34 type SITE sequence P description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 59) chain E residue 35 type SITE sequence C description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 60) chain F residue 34 type SITE sequence P description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 61) chain F residue 35 type SITE sequence C description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 62) chain G residue 34 type SITE sequence P description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 63) chain G residue 35 type SITE sequence C description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 64) chain A residue 35 type SITE sequence C description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 65) chain B residue 34 type SITE sequence P description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 66) chain B residue 35 type SITE sequence C description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 67) chain C residue 34 type SITE sequence P description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 68) chain C residue 35 type SITE sequence C description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 69) chain D residue 34 type SITE sequence P description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 70) chain D residue 35 type SITE sequence C description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 71) chain E residue 34 type SITE sequence P description Contributes to redox potential value source Swiss-Prot : SWS_FT_FI3 72) chain A residue 70 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI4 73) chain B residue 70 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI4 74) chain C residue 70 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI4 75) chain D residue 70 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI4 76) chain E residue 70 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI4 77) chain F residue 70 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI4 78) chain G residue 70 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI4

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