eF-site ID 1ne7-ABCDEF PDB Code 1ne7 Chain A, B, C, D, E, F click to enlarge Title HUMAN GLUCOSAMINE-6-PHOSPHATE DEAMINASE ISOMERASE AT 1.75 A RESOLUTION COMPLEXED WITH N-ACETYL-GLUCOSAMINE-6-PHOSPHATE AND 2-DEOXY-2-AMINO-GLUCITOL-6-PHOSPHATE Classification HYDROLASE Compound Glucosamine-6-phosphate isomerase Source (GNPI_HUMAN) Sequence A:  MKLIILEHYSQASEWAAKYIRNRIIQFNPGPEKYFTLGLP TGSTPLGCYKKLIEYYKNGDLSFKYVKTFNMDEYVGLPRD HPESYHSFMWNNFFKHIDIHPENTHILDGNAVDLQAECDA FEEKIKAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVK TLAMDTILANARFFDGELTKVPTMALTVGVGTVMDAREVM ILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCD EDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKEKETEKS Q B:  MKLIILEHYSQASEWAAKYIRNRIIQFNPGPEKYFTLGLP TGSTPLGCYKKLIEYYKNGDLSFKYVKTFNMDEYVGLPRD HPESYHSFMWNNFFKHIDIHPENTHILDGNAVDLQAECDA FEEKIKAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVK TLAMDTILANARFFDGELTKVPTMALTVGVGTVMDAREVM ILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCD EDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKE C:  MKLIILEHYSQASEWAAKYIRNRIIQFNPGPEKYFTLGLP TGSTPLGCYKKLIEYYKNGDLSFKYVKTFNMDEYVGLPRD HPESYHSFMWNNFFKHIDIHPENTHILDGNAVDLQAECDA FEEKIKAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVK TLAMDTILANARFFDGELTKVPTMALTVGVGTVMDAREVM ILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCD EDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKE D:  MKLIILEHYSQASEWAAKYIRNRIIQFNPGPEKYFTLGLP TGSTPLGCYKKLIEYYKNGDLSFKYVKTFNMDEYVGLPRD HPESYHSFMWNNFFKHIDIHPENTHILDGNAVDLQAECDA FEEKIKAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVK TLAMDTILANARFFDGELTKVPTMALTVGVGTVMDAREVM ILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCD EDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKE E:  MKLIILEHYSQASEWAAKYIRNRIIQFNPGPEKYFTLGLP TGSTPLGCYKKLIEYYKNGDLSFKYVKTFNMDEYVGLPRD HPESYHSFMWNNFFKHIDIHPENTHILDGNAVDLQAECDA FEEKIKAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVK TLAMDTILANARFFDGELTKVPTMALTVGVGTVMDAREVM ILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCD EDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKE F:  MKLIILEHYSQASEWAAKYIRNRIIQFNPGPEKYFTLGLP TGSTPLGCYKKLIEYYKNGDLSFKYVKTFNMDEYVGLPRD HPESYHSFMWNNFFKHIDIHPENTHILDGNAVDLQAECDA FEEKIKAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVK TLAMDTILANARFFDGELTKVPTMALTVGVGTVMDAREVM ILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCD EDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKE Description Functional site 1) chain A residue 141 type ACT_SITE sequence D description For ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 2) chain E residue 148 type ACT_SITE sequence E description For ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 3) chain F residue 141 type ACT_SITE sequence D description For ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 4) chain F residue 148 type ACT_SITE sequence E description For ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 5) chain A residue 148 type ACT_SITE sequence E description For ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 6) chain B residue 141 type ACT_SITE sequence D description For ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 7) chain B residue 148 type ACT_SITE sequence E description For ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 8) chain C residue 141 type ACT_SITE sequence D description For ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 9) chain C residue 148 type ACT_SITE sequence E description For ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 10) chain D residue 141 type ACT_SITE sequence D description For ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 11) chain D residue 148 type ACT_SITE sequence E description For ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 12) chain E residue 141 type ACT_SITE sequence D description For ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 125-143 type prosite sequence IKAAGGIELFVGGIGPDGH description GLC_GALNAC_ISOMERASE Glucosamine/galactosamine-6-phosphate isomerases signature. IkaaGgIeLfVgGIGpDGH source prosite : PS01161 14) chain A residue 72 type ACT_SITE sequence D description Proton acceptor; for enolization step => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 72 type ACT_SITE sequence D description Proton acceptor; for enolization step => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 16) chain C residue 72 type ACT_SITE sequence D description Proton acceptor; for enolization step => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 17) chain D residue 72 type ACT_SITE sequence D description Proton acceptor; for enolization step => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 18) chain E residue 72 type ACT_SITE sequence D description Proton acceptor; for enolization step => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 19) chain F residue 72 type ACT_SITE sequence D description Proton acceptor; for enolization step => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 143 type ACT_SITE sequence H description Proton acceptor; for ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 21) chain B residue 143 type ACT_SITE sequence H description Proton acceptor; for ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 22) chain C residue 143 type ACT_SITE sequence H description Proton acceptor; for ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 23) chain D residue 143 type ACT_SITE sequence H description Proton acceptor; for ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 24) chain E residue 143 type ACT_SITE sequence H description Proton acceptor; for ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 25) chain F residue 143 type ACT_SITE sequence H description Proton acceptor; for ring-opening step => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 64 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 27) chain B residue 64 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 28) chain C residue 64 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 29) chain D residue 64 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 30) chain E residue 64 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 31) chain F residue 64 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 32) chain A residue 161 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:O88958 source Swiss-Prot : SWS_FT_FI5 33) chain B residue 161 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:O88958 source Swiss-Prot : SWS_FT_FI5 34) chain C residue 161 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:O88958 source Swiss-Prot : SWS_FT_FI5 35) chain D residue 161 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:O88958 source Swiss-Prot : SWS_FT_FI5 36) chain E residue 161 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:O88958 source Swiss-Prot : SWS_FT_FI5 37) chain F residue 161 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:O88958 source Swiss-Prot : SWS_FT_FI5

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