eF-site ID 1a0f-AB PDB Code 1a0f Chain A, B click to enlarge Title CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTATHIONESULFONIC ACID Classification TRANSFERASE Compound GLUTATHIONE S-TRANSFERASE Source null (GST_ECOLI) Sequence A:  MKLFYKPGACSLASHITLRESGKDFTLVSVDLMKKRLENG DDYFAVNPKGQVPALLLDDGTLLTEGVAIMQYLADSVPDR QLLAPVNSISRYKTIEWLNYIATELHKGFTPLFRPDTPEE YKPTVRAQLEKKLQYVNEALKDEHWICGQRFTIADAYLFT VLRWAYAVKLNLEGLEHIAAFMQRMAERPEVQDALSAEGL K B:  MKLFYKPGACSLASHITLRESGKDFTLVSVDLMKKRLENG DDYFAVNPKGQVPALLLDDGTLLTEGVAIMQYLADSVPDR QLLAPVNSISRYKTIEWLNYIATELHKGFTPLFRPDTPEE YKPTVRAQLEKKLQYVNEALKDEHWICGQRFTIADAYLFT VLRWAYAVKLNLEGLEHIAAFMQRMAERPEVQDALSAEGL K Description Functional site 1) chain A residue 9 type sequence A description BINDING SITE FOR RESIDUE GTS A 203 source : AC1 2) chain A residue 10 type sequence C description BINDING SITE FOR RESIDUE GTS A 203 source : AC1 3) chain A residue 32 type sequence L description BINDING SITE FOR RESIDUE GTS A 203 source : AC1 4) chain A residue 35 type sequence K description BINDING SITE FOR RESIDUE GTS A 203 source : AC1 5) chain A residue 51 type sequence Q description BINDING SITE FOR RESIDUE GTS A 203 source : AC1 6) chain A residue 52 type sequence V description BINDING SITE FOR RESIDUE GTS A 203 source : AC1 7) chain A residue 65 type sequence E description BINDING SITE FOR RESIDUE GTS A 203 source : AC1 8) chain A residue 66 type sequence G description BINDING SITE FOR RESIDUE GTS A 203 source : AC1 9) chain A residue 106 type sequence H description BINDING SITE FOR RESIDUE GTS A 203 source : AC1 10) chain A residue 107 type sequence K description BINDING SITE FOR RESIDUE GTS A 203 source : AC1 11) chain B residue 99 type sequence N description BINDING SITE FOR RESIDUE GTS A 203 source : AC1 12) chain B residue 103 type sequence T description BINDING SITE FOR RESIDUE GTS A 203 source : AC1 13) chain B residue 104 type sequence E description BINDING SITE FOR RESIDUE GTS A 203 source : AC1 14) chain A residue 99 type sequence N description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 15) chain A residue 103 type sequence T description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 16) chain A residue 104 type sequence E description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 17) chain B residue 9 type sequence A description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 18) chain B residue 10 type sequence C description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 19) chain B residue 32 type sequence L description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 20) chain B residue 35 type sequence K description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 21) chain B residue 51 type sequence Q description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 22) chain B residue 52 type sequence V description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 23) chain B residue 65 type sequence E description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 24) chain B residue 66 type sequence G description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 25) chain B residue 106 type sequence H description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 26) chain B residue 107 type sequence K description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 27) chain B residue 164 type sequence W description BINDING SITE FOR RESIDUE GTS B 203 source : AC2 28) chain A residue 65 type BINDING sequence E description BINDING => ECO:0000305|PubMed:9680481 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 99 type BINDING sequence N description BINDING => ECO:0000305|PubMed:9680481 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 103 type BINDING sequence T description BINDING => ECO:0000305|PubMed:9680481 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 65 type BINDING sequence E description BINDING => ECO:0000305|PubMed:9680481 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 99 type BINDING sequence N description BINDING => ECO:0000305|PubMed:9680481 source Swiss-Prot : SWS_FT_FI1 33) chain B residue 103 type BINDING sequence T description BINDING => ECO:0000305|PubMed:9680481 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 10 type BINDING sequence C description BINDING => ECO:0000305|PubMed:9680481 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 35 type BINDING sequence K description BINDING => ECO:0000305|PubMed:9680481 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 52 type BINDING sequence V description BINDING => ECO:0000305|PubMed:9680481 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 10 type BINDING sequence C description BINDING => ECO:0000305|PubMed:9680481 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 35 type BINDING sequence K description BINDING => ECO:0000305|PubMed:9680481 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 52 type BINDING sequence V description BINDING => ECO:0000305|PubMed:9680481 source Swiss-Prot : SWS_FT_FI1

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