eF-site ID 1vbg-A PDB Code 1vbg Chain A click to enlarge Title Pyruvate Phosphate Dikinase from Maize Classification TRANSFERASE Compound pyruvate,orthophosphate dikinase Source null (PPDK_MAIZE) Sequence A:  KKRVFHFGKGKSEGNKTMKELLGGKGANLAEMASIGLSVP PGFTVSTEACQQYQDAGCALPAGLWAEIVDGLQWVEEYMG ATLGDPQRPLLLSVRSGAAVSMPGMMDTVLNLGLNDEVAA GLAAKSGERFAYDSFRRFLDMFGNVVMDIPRSLFEEKLEH MKESKGLKNDTDLTASDLKELVGQYKEVYLSAKGEPFPSD PKKQLELAVLAVFNSWESPRAKKYRSINQITGLRGTAVNV QCMVFGNMGNTSGTGVLFTRNPNTGEKKLYGEFLVNAQGE DVVAGIRTPEDLDAMKNLMPQAYDELVENCNILESHYKEM QDIEFTVQENRLWMLQCRTGKRTGKSAVKIAVDMVNEGLV EPRSAIKMVEPGHLDQLLHPQFENPSAYKDQVIATGLPAS PGAAVGQVVFTAEDAEAWHSQGKAAILVRAETSPEDVGGM HAAVGILTERGGMTSHAAVVARGWGKCCVSGCSGIRVNDA EKLVTIGGHVLREGEWLSLNGSTGEVILGKQPLSPPALSG DLGTFMAWVDDVRKLKVLANADTPDDALTARNNGAQGIGL CRTEHMFFASDERIKAVRQMIMAPTLELRQQALDRLLPYQ RSDFEGIFRAMDGLPVTIRLLDPPLHEFLPEGNIEDIVSE LCAETGANQEDALARIEKLSEVNPMLGFRGCRLGISYPEL TEMQARAIFEAAIAMTNQGVQVFPEIMVPLVGTPQELGHQ VTLIRQVAEKVFANVGKTIGYKVGTMIEIPRAALVADEIA EQAEFFSFGTNDLTQMTFGYSRDDVGKFIPVYLAQGILQH DPFEVLDQRGVGELVKFATERGRKARPNLKVGICGEHGGE PSSVAFFAKAGLDYVSCSPFRVPIARLAAAQVLV Description Functional site 1) chain A residue 750 type sequence E description BINDING SITE FOR RESIDUE MG A 2000 source : AC1 2) chain A residue 774 type sequence D description BINDING SITE FOR RESIDUE MG A 2000 source : AC1 3) chain A residue 564 type sequence R description BINDING SITE FOR RESIDUE SO4 A 3000 source : AC2 4) chain A residue 621 type sequence R description BINDING SITE FOR RESIDUE SO4 A 3000 source : AC2 5) chain A residue 542 type sequence N description BINDING SITE FOR RESIDUE SO4 A 3001 source : AC3 6) chain A residue 564 type sequence R description BINDING SITE FOR RESIDUE SO4 A 3001 source : AC3 7) chain A residue 837 type sequence G description BINDING SITE FOR RESIDUE SO4 A 3001 source : AC3 8) chain A residue 838 type sequence E description BINDING SITE FOR RESIDUE SO4 A 3001 source : AC3 9) chain A residue 860 type sequence S description BINDING SITE FOR RESIDUE SO4 A 3001 source : AC3 10) chain A residue 519 type sequence A description BINDING SITE FOR RESIDUE SO4 A 3002 source : AC4 11) chain A residue 520 type sequence L description BINDING SITE FOR RESIDUE SO4 A 3002 source : AC4 12) chain A residue 521 type sequence S description BINDING SITE FOR RESIDUE SO4 A 3002 source : AC4 13) chain A residue 458 type ACT_SITE sequence H description Tele-phosphohistidine intermediate => ECO:0000269|PubMed:10683263 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 836 type ACT_SITE sequence C description Proton donor => ECO:0000305|PubMed:15667207 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 453-464 type prosite sequence GGMTSHAAVVAR description PEP_ENZYMES_PHOS_SITE PEP-utilizing enzymes phosphorylation site signature. GGmTsHAAVVAR source prosite : PS00370 16) chain A residue 766-784 type prosite sequence EFFSFGTNDLTQMTFGYSR description PEP_ENZYMES_2 PEP-utilizing enzymes signature 2. EfFSFGTNDLtQMTFGysR source prosite : PS00742 17) chain A residue 750 type BINDING sequence E description BINDING => ECO:0000269|PubMed:15667207 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 771 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15667207 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 772 type BINDING sequence T description BINDING => ECO:0000269|PubMed:15667207 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 773 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15667207 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 774 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15667207 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 564 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15667207 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 621 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15667207 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 238 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:24710069 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 435 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:24710069 source Swiss-Prot : SWS_FT_FI5 26) chain A residue 456 type MOD_RES sequence T description Phosphothreonine; by PDRP1 => ECO:0000269|PubMed:22833285, ECO:0000269|PubMed:24710069, ECO:0000269|PubMed:2834385 source Swiss-Prot : SWS_FT_FI6 27) chain A residue 457 type MOD_RES sequence S description Phosphoserine; by PDRP1 => ECO:0000269|PubMed:24710069 source Swiss-Prot : SWS_FT_FI7

Display surface Download Links