eF-site ID 1ad1-AB PDB Code 1ad1 Chain A, B click to enlarge Title DIHYDROPTEROATE SYNTHETASE (APO FORM) FROM STAPHYLOCOCCUS AUREUS Classification TRANSFERASE Compound DIHYDROPTEROATE SYNTHETASE Source ORGANISM_SCIENTIFIC: Staphylococcus aureus; Sequence A:  TKTKIMGILNVTPDSFSDGGKFNNVESAVTRVKAMMDEGA DIIDVGGVSTRPGHEMITVEEELNRVLPVVEAIVGFDVKI SVDTFRSEVAEACLKLGVDIINDQWAGLYDHRMFQVVAKY DAEIVLMHNGNGNRDEPVVEEMLTSLLAQAHQAKIAGIPS NKIWLDPGIGFAKTRNEEAEVMARLDELVATEYPVLLATS RKRFTKEMMGYDTTPVERDEVTAATTAYGIMKGVRAVRVH NVELNAKLAKGIDFLKENENARHN B:  TKTKIMGILNVTPNVESAVTRVKAMMDEGADIIDVGGVST MITVEEELNRVLPVVEAIVGFDVKISVDTFRSEVAEACLK LGVDIINDQWAGLYDHRMFQVVAKYDAEIVLMHNGNGNRD EPVVEEMLTSLLAQAHQAKIAGIPSNKIWLDPGIGFAKTR NEEAEVMARLDELVATEYPVLLATSRKRFTKEMMGYDTTP VERDEVTAATTAYGIMKGVRAVRVHNVELNAKLAKGIDFL KENENARHNFS Description Functional site 1) chain B residue 75 type sequence V description BINDING SITE FOR RESIDUE K B 1 source : AC1 2) chain B residue 77 type sequence F description BINDING SITE FOR RESIDUE K B 1 source : AC1 3) chain B residue 79 type sequence V description BINDING SITE FOR RESIDUE K B 1 source : AC1 4) chain A residue 75 type sequence V description BINDING SITE FOR RESIDUE K A 268 source : AC2 5) chain A residue 77 type sequence F description BINDING SITE FOR RESIDUE K A 268 source : AC2 6) chain A residue 79 type sequence V description BINDING SITE FOR RESIDUE K A 268 source : AC2 7) chain A residue 96 type sequence K description BINDING SITE FOR RESIDUE TRS A 500 source : AC3 8) chain A residue 11 type BINDING sequence N description BINDING => ECO:0000305|PubMed:9149138 source Swiss-Prot : SWS_FT_FI1 9) chain B residue 11 type BINDING sequence N description BINDING => ECO:0000305|PubMed:9149138 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 52 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9149138, ECO:0007744|PDB:1AD4 source Swiss-Prot : SWS_FT_FI2 11) chain B residue 167 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9149138, ECO:0007744|PDB:1AD4 source Swiss-Prot : SWS_FT_FI2 12) chain B residue 203 type BINDING sequence K description BINDING => ECO:0000305|PubMed:9149138, ECO:0007744|PDB:1AD4 source Swiss-Prot : SWS_FT_FI2 13) chain B residue 239 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9149138, ECO:0007744|PDB:1AD4 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 84 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9149138, ECO:0007744|PDB:1AD4 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 103 type BINDING sequence N description BINDING => ECO:0000305|PubMed:9149138, ECO:0007744|PDB:1AD4 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 167 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9149138, ECO:0007744|PDB:1AD4 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 203 type BINDING sequence K description BINDING => ECO:0000305|PubMed:9149138, ECO:0007744|PDB:1AD4 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 239 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9149138, ECO:0007744|PDB:1AD4 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 84 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9149138, ECO:0007744|PDB:1AD4 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 103 type BINDING sequence N description BINDING => ECO:0000305|PubMed:9149138, ECO:0007744|PDB:1AD4 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 6-21 type prosite sequence IMGILNVTPDSFSDGG description DHPS_1 Dihydropteroate synthase signature 1. ImGILNvTpDSFsDgG source prosite : PS00792 22) chain A residue 40-53 type prosite sequence GADIIDVGGVSTRP description DHPS_2 Dihydropteroate synthase signature 2. GAdIIDVGGvsTrP source prosite : PS00793

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