eF-site ID 1dkm-A PDB Code 1dkm Chain A click to enlarge Title CRYSTAL STRUCTURE OF ESCHERICHIA COLI PHYTASE AT PH 6.6 WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGE Classification HYDROLASE Compound PHYTASE Source (PPA_ECOLI) Sequence A:  QSEPELKLESVVIVSRHGVRAPTKATQLMQDVTPDAWPTW PVKLGWLTPRGGELIAYLGHYQRQRLVADGLLAKKGCPQS GQVAIIADVDERTRKTGEAFAAGLAPDCAITVHTQTDTSS PDPLFNPLKTGVCQLDNANVTDAILSRAGGSIADFTGHRQ TAFRELERVLNFPQSNLCLKREKQDESCSLTQALPSELKV SADNVSLTGAVSLASMLTEIFLLQQAQGMPEPGWGRITDS HQWNTLLSLHNAQFYLLQRTPEVARSRATPLLDLIKTALT PHPPQKQAYGVTLPTSVLFIAGHDTNLANLGGALELNWTL PGQPDNTPPGGELVFERWRRLSDNSQWIQVSLVFQTLQQM RDKTPLSLNTPPGEVKLTLAGCEERNAQGMCSLAGFTQIV NEARIPACSL Description Functional site 1) chain A residue 113 type sequence H description BINDING SITE FOR RESIDUE HG A 500 source : AC1 2) chain A residue 154 type sequence D description BINDING SITE FOR RESIDUE HG A 500 source : AC1 3) chain A residue 158 type sequence H description BINDING SITE FOR RESIDUE HG A 500 source : AC1 4) chain A residue 289 type sequence Y description BINDING SITE FOR RESIDUE HG A 500 source : AC1 5) chain A residue 8-22 type prosite sequence LESVVIVSRHGVRAP description HIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. LesVviVsRHGvRaP source prosite : PS00616 6) chain A residue 297-313 type prosite sequence VLFIAGHDTNLANLGGA description HIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. VlFIaGHDTNLanLggA source prosite : PS00778 7) chain A residue 17 type ACT_SITE sequence H description Nucleophile => ECO:0000305|PubMed:10655611, ECO:0000305|PubMed:1429631 source Swiss-Prot : SWS_FT_FI1 8) chain A residue 304 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:10655611, ECO:0000305|PubMed:8407904 source Swiss-Prot : SWS_FT_FI2 9) chain A residue 16 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10655611, ECO:0000305|Ref.18, ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ source Swiss-Prot : SWS_FT_FI3 10) chain A residue 20 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10655611, ECO:0000305|Ref.18, ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ source Swiss-Prot : SWS_FT_FI3 11) chain A residue 92 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10655611, ECO:0000305|Ref.18, ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ source Swiss-Prot : SWS_FT_FI3 12) chain A residue 303 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10655611, ECO:0000305|Ref.18, ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ source Swiss-Prot : SWS_FT_FI3 13) chain A residue 267 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10655611, ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ source Swiss-Prot : SWS_FT_FI4

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