eF-site ID 2fpw-B PDB Code 2fpw Chain B click to enlarge Title Crystal Structure of the N-terminal Domain of E.coli HisB- Phosphoaspartate intermediate. Classification HYDROLASE Compound Histidine biosynthesis bifunctional protein hisB Source Escherichia coli O157:H7 (HIS7_ECO57) Sequence B:  QKYLFIXRDGTLISEPPSDFQVDRFDKLAFEPGVIPQLLK LQKAGYKLVMITNQDGLGTQSFPQADFDGPHNLMMQIFTS QGVQFDEVLICPHLPADECDCRKPKVKLVERYLAEQAMDR ANSYVIGDRATDIQLAENMGINGLRYDRETLNWPMIGEQL TRR Description Functional site 1) chain B residue 94 type sequence C description BINDING SITE FOR RESIDUE ZN B 501 source : AC1 2) chain B residue 96 type sequence H description BINDING SITE FOR RESIDUE ZN B 501 source : AC1 3) chain B residue 102 type sequence C description BINDING SITE FOR RESIDUE ZN B 501 source : AC1 4) chain B residue 104 type sequence C description BINDING SITE FOR RESIDUE ZN B 501 source : AC1 5) chain B residue 105 type sequence R description BINDING SITE FOR RESIDUE ZN B 501 source : AC1 6) chain B residue 12 type sequence D description BINDING SITE FOR RESIDUE CA B 504 source : AC4 7) chain B residue 23 type sequence F description BINDING SITE FOR RESIDUE CA B 504 source : AC4 8) chain B residue 10 type sequence X description BINDING SITE FOR RESIDUE CA B 505 source : AC5 9) chain B residue 12 type sequence D description BINDING SITE FOR RESIDUE CA B 505 source : AC5 10) chain B residue 131 type sequence D description BINDING SITE FOR RESIDUE CA B 505 source : AC5 11) chain B residue 94 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 12) chain B residue 96 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 102 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 14) chain B residue 104 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 15) chain B residue 131 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 10 type BINDING sequence X description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 17) chain B residue 12 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 18) chain B residue 10 type ACT_SITE sequence X description Nucleophile => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000305|PubMed:16966333 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 12 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000305|PubMed:16966333 source Swiss-Prot : SWS_FT_FI2

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