eF-site ID 1ney-AB PDB Code 1ney Chain A, B click to enlarge Title Triosephosphate Isomerase in Complex with DHAP Classification ISOMERASE Compound triosephosphate isomerase Source null (TPIS_YEAST) Sequence A:  ARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVIC PPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVD QIKDVGAKYVILGHSERRSYFHEDDKFIADKTKFALGQGV GVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDFTNVV VAYEPVXAIGTGLAATPEDAQDIHASIRKFLASKLGDKAA SELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEFV DIINSRN B:  ARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVIC PPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVD QIKDVGAKYVILGHSERRSYFHEDDKFIADKTKFALGQGV GVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDFTNVV VAYEPVXAIGTGLAATPEDAQDIHASIRKFLASKLGDKAA SELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEFV DIINSRN Description Functional site 1) chain A residue 10 type sequence N description BINDING SITE FOR RESIDUE 13P A 5001 source : AC1 2) chain A residue 12 type sequence K description BINDING SITE FOR RESIDUE 13P A 5001 source : AC1 3) chain A residue 95 type sequence H description BINDING SITE FOR RESIDUE 13P A 5001 source : AC1 4) chain A residue 165 type sequence E description BINDING SITE FOR RESIDUE 13P A 5001 source : AC1 5) chain A residue 169 type sequence A description BINDING SITE FOR RESIDUE 13P A 5001 source : AC1 6) chain A residue 170 type sequence I description BINDING SITE FOR RESIDUE 13P A 5001 source : AC1 7) chain A residue 171 type sequence G description BINDING SITE FOR RESIDUE 13P A 5001 source : AC1 8) chain A residue 211 type sequence S description BINDING SITE FOR RESIDUE 13P A 5001 source : AC1 9) chain A residue 230 type sequence L description BINDING SITE FOR RESIDUE 13P A 5001 source : AC1 10) chain A residue 232 type sequence G description BINDING SITE FOR RESIDUE 13P A 5001 source : AC1 11) chain A residue 233 type sequence G description BINDING SITE FOR RESIDUE 13P A 5001 source : AC1 12) chain B residue 10 type sequence N description BINDING SITE FOR RESIDUE 13P B 6001 source : AC2 13) chain B residue 12 type sequence K description BINDING SITE FOR RESIDUE 13P B 6001 source : AC2 14) chain B residue 95 type sequence H description BINDING SITE FOR RESIDUE 13P B 6001 source : AC2 15) chain B residue 165 type sequence E description BINDING SITE FOR RESIDUE 13P B 6001 source : AC2 16) chain B residue 169 type sequence A description BINDING SITE FOR RESIDUE 13P B 6001 source : AC2 17) chain B residue 170 type sequence I description BINDING SITE FOR RESIDUE 13P B 6001 source : AC2 18) chain B residue 171 type sequence G description BINDING SITE FOR RESIDUE 13P B 6001 source : AC2 19) chain B residue 211 type sequence S description BINDING SITE FOR RESIDUE 13P B 6001 source : AC2 20) chain B residue 230 type sequence L description BINDING SITE FOR RESIDUE 13P B 6001 source : AC2 21) chain B residue 232 type sequence G description BINDING SITE FOR RESIDUE 13P B 6001 source : AC2 22) chain B residue 233 type sequence G description BINDING SITE FOR RESIDUE 13P B 6001 source : AC2 23) chain A residue 11 type BINDING sequence F description BINDING => ECO:0000269|PubMed:12509510 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 13 type BINDING sequence L description BINDING => ECO:0000269|PubMed:12509510 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 11 type BINDING sequence F description BINDING => ECO:0000269|PubMed:12509510 source Swiss-Prot : SWS_FT_FI3 26) chain B residue 13 type BINDING sequence L description BINDING => ECO:0000269|PubMed:12509510 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 5 type MOD_RES sequence F description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI4 28) chain B residue 5 type MOD_RES sequence F description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 72 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 30) chain A residue 216 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 31) chain B residue 72 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 32) chain B residue 216 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 33) chain B residue 224 type CROSSLNK sequence A description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI6 34) chain A residue 224 type CROSSLNK sequence A description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI6 35) chain A residue 163-173 type prosite sequence AYEPVXAIGTG description TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG source prosite : PS00171 36) chain A residue 96 type ACT_SITE sequence S description Electrophile source Swiss-Prot : SWS_FT_FI1 37) chain B residue 96 type ACT_SITE sequence S description Electrophile source Swiss-Prot : SWS_FT_FI1 38) chain A residue 166 type ACT_SITE sequence P description Proton acceptor source Swiss-Prot : SWS_FT_FI2 39) chain B residue 166 type ACT_SITE sequence P description Proton acceptor source Swiss-Prot : SWS_FT_FI2

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