eF-site ID 2cxn-AB PDB Code 2cxn Chain A, B click to enlarge Title Crystal structure of mouse AMF / phosphate complex Classification ISOMERASE Compound Glucose-6-phosphate isomerase Source Mus musculus (Mouse) (G6PI_MOUSE) Sequence A:  MAALTRNPQFQKLLEWHRANSANLKLRELFEADPERFNNF SLNLNTNHGHILVDYSKNLVSKEVMQMLVELAKSRGVEAA RDNMFSGSKINYTEDRAVLHVALRNRSNTPIKVDGKDVMP EVNRVLDKMKSFCQRVRSGDWKGYTGKSITDIINIGIGGS DLGPLMVTEALKPYSKGGPRVWFVSNIDGTHIAKTLASLS PETSLFIIASKTFTTQETITNAETAKEWFLEAAKDPSAVA KHFVALSTNTAKVKEFGIDPQNMFEFWDWVGGRYSLWSAI GLSIALHVGFDHFEQLLSGAHWMDQHFLKTPLEKNAPVLL ALLGIWYINCYGCETHALLPYDQYMHRFAAYFQQGDMESN GKYITKSGARVDHQTGPIVWGEPGTNGQHAFYQLIHQGTK MIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMKGK LPEEARKELQAAGKSPEDLEKLLPHKVFEGNRPTNSIVFT KLTPFILGALIAMYEHKIFVQGIMWDINSFDQWGVELGKQ LAKKIEPELEGSSAVTSHDSSTNGLISFIKQQRDTKL B:  MAALTRNPQFQKLLEWHRANSANLKLRELFEADPERFNNF SLNLNTNHGHILVDYSKNLVSKEVMQMLVELAKSRGVEAA RDNMFSGSKINYTEDRAVLHVALRNRSNTPIKVDGKDVMP EVNRVLDKMKSFCQRVRSGDWKGYTGKSITDIINIGIGGS DLGPLMVTEALKPYSKGGPRVWFVSNIDGTHIAKTLASLS PETSLFIIASKTFTTQETITNAETAKEWFLEAAKDPSAVA KHFVALSTNTAKVKEFGIDPQNMFEFWDWVGGRYSLWSAI GLSIALHVGFDHFEQLLSGAHWMDQHFLKTPLEKNAPVLL ALLGIWYINCYGCETHALLPYDQYMHRFAAYFQQGDMESN GKYITKSGARVDHQTGPIVWGEPGTNGQHAFYQLIHQGTK MIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMKGK LPEEARKELQAAGKSPEDLEKLLPHKVFEGNRPTNSIVFT KLTPFILGALIAMYEHKIFVQGIMWDINSFDQWGVELGKQ LAKKIEPELEGSSAVTSHDSSTNGLISFIKQQRDTKL Description Functional site 1) chain A residue 160 type sequence S description BINDING SITE FOR RESIDUE PO4 A 1601 source : AC1 2) chain A residue 210 type sequence S description BINDING SITE FOR RESIDUE PO4 A 1601 source : AC1 3) chain A residue 211 type sequence K description BINDING SITE FOR RESIDUE PO4 A 1601 source : AC1 4) chain A residue 212 type sequence T description BINDING SITE FOR RESIDUE PO4 A 1601 source : AC1 5) chain A residue 215 type sequence T description BINDING SITE FOR RESIDUE PO4 A 1601 source : AC1 6) chain A residue 140 type sequence D description BINDING SITE FOR RESIDUE GOL A 1701 source : AC2 7) chain A residue 141 type sequence W description BINDING SITE FOR RESIDUE GOL A 1701 source : AC2 8) chain A residue 142 type sequence K description BINDING SITE FOR RESIDUE GOL A 1701 source : AC2 9) chain A residue 241 type sequence K description BINDING SITE FOR RESIDUE GOL A 1701 source : AC2 10) chain A residue 549 type sequence I description BINDING SITE FOR RESIDUE GOL B 1702 source : AC3 11) chain A residue 553 type sequence R description BINDING SITE FOR RESIDUE GOL B 1702 source : AC3 12) chain B residue 419 type sequence G description BINDING SITE FOR RESIDUE GOL B 1702 source : AC3 13) chain B residue 422 type sequence H description BINDING SITE FOR RESIDUE GOL B 1702 source : AC3 14) chain B residue 423 type sequence K description BINDING SITE FOR RESIDUE GOL B 1702 source : AC3 15) chain B residue 426 type sequence L description BINDING SITE FOR RESIDUE GOL B 1702 source : AC3 16) chain B residue 135 type sequence R description BINDING SITE FOR RESIDUE GOL B 1703 source : AC4 17) chain B residue 141 type sequence W description BINDING SITE FOR RESIDUE GOL B 1703 source : AC4 18) chain B residue 142 type sequence K description BINDING SITE FOR RESIDUE GOL B 1703 source : AC4 19) chain A residue 419 type sequence G description BINDING SITE FOR RESIDUE GOL A 1704 source : AC5 20) chain A residue 422 type sequence H description BINDING SITE FOR RESIDUE GOL A 1704 source : AC5 21) chain A residue 423 type sequence K description BINDING SITE FOR RESIDUE GOL A 1704 source : AC5 22) chain A residue 426 type sequence L description BINDING SITE FOR RESIDUE GOL A 1704 source : AC5 23) chain B residue 553 type sequence R description BINDING SITE FOR RESIDUE GOL A 1704 source : AC5 24) chain A residue 359 type ACT_SITE sequence S description Proton donor => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 359 type ACT_SITE sequence S description Proton donor => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 390 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 520 type ACT_SITE sequence Q description ACT_SITE => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI2 28) chain B residue 390 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI2 29) chain B residue 520 type ACT_SITE sequence Q description ACT_SITE => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 160 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT source Swiss-Prot : SWS_FT_FI3 31) chain B residue 359 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT source Swiss-Prot : SWS_FT_FI3 32) chain B residue 390 type BINDING sequence A description BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT source Swiss-Prot : SWS_FT_FI3 33) chain B residue 520 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT source Swiss-Prot : SWS_FT_FI3 34) chain A residue 211 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT source Swiss-Prot : SWS_FT_FI3 35) chain A residue 355 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT source Swiss-Prot : SWS_FT_FI3 36) chain A residue 359 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT source Swiss-Prot : SWS_FT_FI3 37) chain A residue 390 type BINDING sequence A description BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT source Swiss-Prot : SWS_FT_FI3 38) chain A residue 520 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT source Swiss-Prot : SWS_FT_FI3 39) chain B residue 160 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT source Swiss-Prot : SWS_FT_FI3 40) chain B residue 211 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT source Swiss-Prot : SWS_FT_FI3 41) chain B residue 355 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT source Swiss-Prot : SWS_FT_FI3 42) chain A residue 3 type MOD_RES sequence A description N-acetylalanine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI4 43) chain B residue 3 type MOD_RES sequence A description N-acetylalanine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI4 44) chain A residue 13 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI5 45) chain B residue 13 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI5 46) chain A residue 87 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:Q6P6V0 source Swiss-Prot : SWS_FT_FI6 47) chain B residue 87 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:Q6P6V0 source Swiss-Prot : SWS_FT_FI6 48) chain A residue 108 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI7 49) chain B residue 108 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI7 50) chain A residue 110 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI8 51) chain B residue 110 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI8 52) chain A residue 143 type MOD_RES sequence G description N6-acetyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI9 53) chain B residue 143 type MOD_RES sequence G description N6-acetyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI9 54) chain A residue 186 type MOD_RES sequence N description Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI10 55) chain B residue 186 type MOD_RES sequence N description Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI10 56) chain A residue 251 type MOD_RES sequence A description Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0 source Swiss-Prot : SWS_FT_FI11 57) chain B residue 251 type MOD_RES sequence A description Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0 source Swiss-Prot : SWS_FT_FI11 58) chain A residue 455 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI12 59) chain B residue 455 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI12 60) chain A residue 456 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI13 61) chain B residue 456 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI13 62) chain A residue 502-519 type prosite sequence GIMWDINSFDQWGVELGK description P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GiMWdinsFDQwGVElgK source prosite : PS00174 63) chain A residue 268-281 type prosite sequence DWVGGRYSLWSAIG description P_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG source prosite : PS00765

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