eF-site ID 2fpw-AB PDB Code 2fpw Chain A, 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 null (HIS7_ECO57) Sequence A:  SQKYLFIXRDGTLISEPDFQVDRFDKLAFEPGVIPQLLKL QKAGYKLVMITNQDGLGTQSFPQADFDGPHNLMMQIFTSQ GVQFDEVLICPHLPADECDCRKPKVKLVERYLMDRANSYV IGDRATDIQLAENMGINGLRYDRETLNWPMIGEQLT 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 A residue 94 type sequence C description BINDING SITE FOR RESIDUE ZN A 502 source : AC2 7) chain A residue 96 type sequence H description BINDING SITE FOR RESIDUE ZN A 502 source : AC2 8) chain A residue 102 type sequence C description BINDING SITE FOR RESIDUE ZN A 502 source : AC2 9) chain A residue 104 type sequence C description BINDING SITE FOR RESIDUE ZN A 502 source : AC2 10) chain A residue 105 type sequence R description BINDING SITE FOR RESIDUE ZN A 502 source : AC2 11) chain A residue 10 type sequence X description BINDING SITE FOR RESIDUE CA A 503 source : AC3 12) chain A residue 12 type sequence D description BINDING SITE FOR RESIDUE CA A 503 source : AC3 13) chain A residue 131 type sequence D description BINDING SITE FOR RESIDUE CA A 503 source : AC3 14) chain B residue 12 type sequence D description BINDING SITE FOR RESIDUE CA B 504 source : AC4 15) chain B residue 23 type sequence F description BINDING SITE FOR RESIDUE CA B 504 source : AC4 16) chain B residue 10 type sequence X description BINDING SITE FOR RESIDUE CA B 505 source : AC5 17) chain B residue 12 type sequence D description BINDING SITE FOR RESIDUE CA B 505 source : AC5 18) chain B residue 131 type sequence D description BINDING SITE FOR RESIDUE CA B 505 source : AC5 19) chain A 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 20) 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 21) chain A 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 22) 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 23) chain A residue 10 type BINDING sequence X description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 12 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 94 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 96 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 27) 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 28) 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 29) 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 30) 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 31) 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 32) chain A residue 102 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 104 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 131 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 source Swiss-Prot : SWS_FT_FI3 35) 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 36) 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

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