eF-site ID 2fd8-AB PDB Code 2fd8 Chain A, B click to enlarge Title Crystal Structure of AlkB in complex with Fe(II), 2-oxoglutarate, and methylated trinucleotide T-meA-T Classification OXIDOREDUCTASE/DNA Compound 5'-D(P*TP*(MA7)P*T)-3' Source Escherichia coli (strain K12) (2FD8) Sequence A:  LAAGAVILRRFAFNAAEQLIRDINDVASQSPFRQMVTPGG YTMSVAMTNCGHLGWTTHRQGYLYSPIDPQTNKPWPAMPQ SFHNLCQRAATAAGYPDFQPDACLINRYAPGAKLSLHQDK DEPDLRAPIVSVSLGLPAIFQFGGLKRNDPLKRLLLEHGD VVVWGGESRLFYHGIQPLKAGFHPLTIDCRYNLTFRQAGK B:  TXT Description Functional site 1) chain A residue 131 type sequence H description BINDING SITE FOR RESIDUE FE2 A 300 source : AC1 2) chain A residue 133 type sequence D description BINDING SITE FOR RESIDUE FE2 A 300 source : AC1 3) chain A residue 187 type sequence H description BINDING SITE FOR RESIDUE FE2 A 300 source : AC1 4) chain A residue 118 type sequence L description BINDING SITE FOR RESIDUE AKG A 400 source : AC2 5) chain A residue 120 type sequence N description BINDING SITE FOR RESIDUE AKG A 400 source : AC2 6) chain A residue 122 type sequence Y description BINDING SITE FOR RESIDUE AKG A 400 source : AC2 7) chain A residue 131 type sequence H description BINDING SITE FOR RESIDUE AKG A 400 source : AC2 8) chain A residue 133 type sequence D description BINDING SITE FOR RESIDUE AKG A 400 source : AC2 9) chain A residue 187 type sequence H description BINDING SITE FOR RESIDUE AKG A 400 source : AC2 10) chain A residue 189 type sequence I description BINDING SITE FOR RESIDUE AKG A 400 source : AC2 11) chain A residue 204 type sequence R description BINDING SITE FOR RESIDUE AKG A 400 source : AC2 12) chain A residue 206 type sequence N description BINDING SITE FOR RESIDUE AKG A 400 source : AC2 13) chain A residue 210 type sequence R description BINDING SITE FOR RESIDUE AKG A 400 source : AC2 14) chain B residue 502 type sequence X description BINDING SITE FOR RESIDUE AKG A 400 source : AC2 15) chain A residue 69 type BINDING sequence W description BINDING => ECO:0000269|PubMed:16482161, ECO:0000269|PubMed:20084272 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 135 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16482161, ECO:0000269|PubMed:20084272 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 161 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16482161, ECO:0000269|PubMed:20084272 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 76 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 19) chain A residue 120 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 20) chain A residue 204 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 21) chain A residue 131 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:16482161 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 133 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:16482161 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 187 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:16482161 source Swiss-Prot : SWS_FT_FI3

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