eF-site ID 1dkp-A PDB Code 1dkp Chain A click to enlarge Title CRYSTAL STRUCTURE OF PHYTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6. PHYTATE IS BOUND WITH ITS 3-PHOSPHATE IN THE ACTIVE SITE. HG2+ CATION ACTS AS AN INTERMOLECULAR BRIDGE Classification HYDROLASE Compound PHYTASE Source (PPA_ECOLI) Sequence A:  QSEPELKLESVVIVSRAGVRAPTKATQLMQDVTPDAWPTW 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 282 type sequence H description BINDING SITE FOR RESIDUE HG A 501 source : AC2 6) chain A residue 285 type sequence Q description BINDING SITE FOR RESIDUE HG A 501 source : AC2 7) chain A residue 287 type sequence Q description BINDING SITE FOR RESIDUE HG A 501 source : AC2 8) chain A residue 293 type sequence L description BINDING SITE FOR RESIDUE HG A 501 source : AC2 9) chain A residue 16 type sequence R description BINDING SITE FOR RESIDUE HG A 502 source : AC3 10) chain A residue 219 type sequence E description BINDING SITE FOR RESIDUE HG A 502 source : AC3 11) chain A residue 250 type sequence H description BINDING SITE FOR RESIDUE HG A 502 source : AC3 12) chain A residue 304 type sequence D description BINDING SITE FOR RESIDUE HG A 502 source : AC3 13) chain A residue 325 type sequence D description BINDING SITE FOR RESIDUE HG A 502 source : AC3 14) chain A residue 327 type sequence T description BINDING SITE FOR RESIDUE HG A 502 source : AC3 15) chain A residue 250 type sequence H description BINDING SITE FOR RESIDUE HG A 503 source : AC4 16) chain A residue 304 type sequence D description BINDING SITE FOR RESIDUE HG A 503 source : AC4 17) chain A residue 325 type sequence D description BINDING SITE FOR RESIDUE HG A 503 source : AC4 18) chain A residue 327 type sequence T description BINDING SITE FOR RESIDUE HG A 503 source : AC4 19) chain A residue 16 type sequence R description BINDING SITE FOR RESIDUE IHP A 550 source : AC5 20) chain A residue 20 type sequence R description BINDING SITE FOR RESIDUE IHP A 550 source : AC5 21) chain A residue 23 type sequence T description BINDING SITE FOR RESIDUE IHP A 550 source : AC5 22) chain A residue 24 type sequence K description BINDING SITE FOR RESIDUE IHP A 550 source : AC5 23) chain A residue 90 type sequence D description BINDING SITE FOR RESIDUE IHP A 550 source : AC5 24) chain A residue 92 type sequence R description BINDING SITE FOR RESIDUE IHP A 550 source : AC5 25) chain A residue 216 type sequence M description BINDING SITE FOR RESIDUE IHP A 550 source : AC5 26) chain A residue 250 type sequence H description BINDING SITE FOR RESIDUE IHP A 550 source : AC5 27) chain A residue 254 type sequence F description BINDING SITE FOR RESIDUE IHP A 550 source : AC5 28) chain A residue 267 type sequence R description BINDING SITE FOR RESIDUE IHP A 550 source : AC5 29) chain A residue 303 type sequence H description BINDING SITE FOR RESIDUE IHP A 550 source : AC5 30) chain A residue 304 type sequence D description BINDING SITE FOR RESIDUE IHP A 550 source : AC5 31) chain A residue 305 type sequence T description BINDING SITE FOR RESIDUE IHP A 550 source : AC5 32) chain A residue 297-313 type prosite sequence VLFIAGHDTNLANLGGA description HIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. VlFIaGHDTNLanLggA source prosite : PS00778 33) chain A residue 17 type ACT_SITE sequence A description Nucleophile => ECO:0000305|PubMed:10655611, ECO:0000305|PubMed:1429631 source Swiss-Prot : SWS_FT_FI1 34) 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 35) 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 36) 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 37) 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 38) 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 39) 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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