eF-site ID 2jgq-A PDB Code 2jgq Chain A click to enlarge Title Kinetics and structural properties of triosephosphate isomerase from Helicobacter pylori Classification ISOMERASE Compound TRIOSEPHOSPHATE ISOMERASE Source null (TPIS_HELPY) Sequence A:  TKIAMANFKSAMPIFKSHAYLKELEKTLKPQHFDRVFVFP DFFGLLPNSFLHFTLGVQNAYPRDCGAFTGEITSKHLEEL KIHTLLIGHSERRTLLKESPSFLKEKFDFFKSKNFKIVYC IGEELTTREKGFKAVKEFLSEQLENIDLNYPNLVVAYEPI WAIGTKSASLEDIYLTHGFLKQILNQKTPLLYGGSVNTQN AKEILGIDSVDGLLIGSASWELENFKTIISFL Description Functional site 1) chain A residue 129 type sequence R description BINDING SITE FOR RESIDUE QGA A1235 source : AC1 2) chain A residue 162 type sequence W description BINDING SITE FOR RESIDUE QGA A1235 source : AC1 3) chain A residue 169 type sequence S description BINDING SITE FOR RESIDUE QGA A1235 source : AC1 4) chain A residue 171 type sequence S description BINDING SITE FOR RESIDUE QGA A1235 source : AC1 5) chain A residue 173 type sequence E description BINDING SITE FOR RESIDUE QGA A1235 source : AC1 6) chain A residue 174 type sequence D description BINDING SITE FOR RESIDUE QGA A1235 source : AC1 7) chain A residue 10 type sequence K description BINDING SITE FOR RESIDUE PO4 A1236 source : AC2 8) chain A residue 163 type sequence A description BINDING SITE FOR RESIDUE PO4 A1236 source : AC2 9) chain A residue 164 type sequence I description BINDING SITE FOR RESIDUE PO4 A1236 source : AC2 10) chain A residue 165 type sequence G description BINDING SITE FOR RESIDUE PO4 A1236 source : AC2 11) chain A residue 197 type sequence S description BINDING SITE FOR RESIDUE PO4 A1236 source : AC2 12) chain A residue 218 type sequence G description BINDING SITE FOR RESIDUE PO4 A1236 source : AC2 13) chain A residue 219 type sequence S description BINDING SITE FOR RESIDUE PO4 A1236 source : AC2 14) chain A residue 90 type ACT_SITE sequence H description Electrophile => ECO:0000255|HAMAP-Rule:MF_00147 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 159 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00147 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 197 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:17957775 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 218 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:17957775 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 8 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:17957775 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 165 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:17957775 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 157-167 type prosite sequence AYEPIWAIGTK description TIM_1 Triosephosphate isomerase active site. AYEPIWAIGTK source prosite : PS00171

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