eF-site ID 1qjc-A PDB Code 1qjc Chain A click to enlarge Title Phosphopantetheine Adenylyltransferase from Escherichia coli in complex with 4'-phosphopantetheine Classification COENZYME A BIOSYNTHESIS Compound PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE Source ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; Sequence A:  KRAIYPGTFDPITNGHIDIVTRATQMFDHVILAIAASPSK KPMFTLEERVALAQQATAHLGNVEVVGFSDLMANFARNQH ATVLIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSK EWSFISSSLVKEVARHQGDVTHFLPENVHQALMAKLA Description Functional site 1) chain A residue 121 type sequence S description BINDING SITE FOR RESIDUE SO4 A1160 source : AC1 2) chain A residue 122 type sequence K description BINDING SITE FOR RESIDUE SO4 A1160 source : AC1 3) chain A residue 18 type sequence H description BINDING SITE FOR RESIDUE SO4 A1161 source : AC2 4) chain A residue 91 type sequence R description BINDING SITE FOR RESIDUE SO4 A1161 source : AC2 5) chain A residue 128 type sequence S description BINDING SITE FOR RESIDUE SO4 A1161 source : AC2 6) chain A residue 129 type sequence S description BINDING SITE FOR RESIDUE SO4 A1161 source : AC2 7) chain A residue 104 type sequence H description BINDING SITE FOR RESIDUE SO4 B1160 source : AC3 8) chain A residue 107 type sequence R description BINDING SITE FOR RESIDUE SO4 B1160 source : AC3 9) chain A residue 18 type catalytic sequence H description 299 source MCSA : MCSA1 10) chain A residue 42 type catalytic sequence K description 299 source MCSA : MCSA1 11) chain A residue 91 type catalytic sequence R description 299 source MCSA : MCSA1 12) chain A residue 129 type catalytic sequence S description 299 source MCSA : MCSA1 13) chain A residue 18 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11812124, ECO:0007744|PDB:1GN8 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 89 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11812124, ECO:0007744|PDB:1GN8 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 99 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11812124, ECO:0007744|PDB:1GN8 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 124 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11812124, ECO:0007744|PDB:1GN8 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 7 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:11812124, ECO:0007744|PDB:1GN8 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 88 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11812124, ECO:0007744|PDB:1QJC source Swiss-Prot : SWS_FT_FI3 19) chain A residue 10 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11812124, ECO:0000269|PubMed:12837781, ECO:0007744|PDB:1H1T, ECO:0007744|PDB:1QJC source Swiss-Prot : SWS_FT_FI1 20) chain A residue 42 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11812124, ECO:0000269|PubMed:12837781, ECO:0007744|PDB:1H1T, ECO:0007744|PDB:1QJC source Swiss-Prot : SWS_FT_FI1 21) chain A residue 74 type BINDING sequence M description BINDING => ECO:0000269|PubMed:11812124, ECO:0000269|PubMed:12837781, ECO:0007744|PDB:1H1T, ECO:0007744|PDB:1QJC source Swiss-Prot : SWS_FT_FI1 22) chain A residue 18 type SITE sequence H description Transition state stabilizer => ECO:0000305|PubMed:11812124 source Swiss-Prot : SWS_FT_FI4

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