eF-site ID 2cxo-AB PDB Code 2cxo Chain A, B click to enlarge Title Crystal structure of mouse AMF / E4P complex Classification ISOMERASE Compound Glucose-6-phosphate isomerase Source null (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 157 type sequence I description BINDING SITE FOR RESIDUE DER A 1601 source : AC1 2) chain A residue 158 type sequence G description BINDING SITE FOR RESIDUE DER A 1601 source : AC1 3) chain A residue 159 type sequence G description BINDING SITE FOR RESIDUE DER A 1601 source : AC1 4) chain A residue 160 type sequence S description BINDING SITE FOR RESIDUE DER A 1601 source : AC1 5) chain A residue 210 type sequence S description BINDING SITE FOR RESIDUE DER A 1601 source : AC1 6) chain A residue 211 type sequence K description BINDING SITE FOR RESIDUE DER A 1601 source : AC1 7) chain A residue 212 type sequence T description BINDING SITE FOR RESIDUE DER A 1601 source : AC1 8) chain A residue 215 type sequence T description BINDING SITE FOR RESIDUE DER A 1601 source : AC1 9) chain A residue 354 type sequence Q description BINDING SITE FOR RESIDUE DER A 1601 source : AC1 10) chain A residue 358 type sequence E description BINDING SITE FOR RESIDUE DER A 1601 source : AC1 11) chain A residue 519 type sequence K description BINDING SITE FOR RESIDUE DER A 1601 source : AC1 12) chain B residue 389 type sequence H description BINDING SITE FOR RESIDUE DER A 1601 source : AC1 13) chain A residue 389 type sequence H description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 14) chain B residue 157 type sequence I description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 15) chain B residue 158 type sequence G description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 16) chain B residue 159 type sequence G description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 17) chain B residue 160 type sequence S description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 18) chain B residue 210 type sequence S description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 19) chain B residue 211 type sequence K description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 20) chain B residue 212 type sequence T description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 21) chain B residue 215 type sequence T description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 22) chain B residue 354 type sequence Q description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 23) chain B residue 358 type sequence E description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 24) chain A residue 140 type sequence D description BINDING SITE FOR RESIDUE GOL A 1701 source : AC3 25) chain A residue 141 type sequence W description BINDING SITE FOR RESIDUE GOL A 1701 source : AC3 26) chain A residue 142 type sequence K description BINDING SITE FOR RESIDUE GOL A 1701 source : AC3 27) chain A residue 241 type sequence K description BINDING SITE FOR RESIDUE GOL A 1701 source : AC3 28) chain A residue 549 type sequence I description BINDING SITE FOR RESIDUE GOL B 1702 source : AC4 29) chain A residue 553 type sequence R description BINDING SITE FOR RESIDUE GOL B 1702 source : AC4 30) chain B residue 419 type sequence G description BINDING SITE FOR RESIDUE GOL B 1702 source : AC4 31) chain B residue 423 type sequence K description BINDING SITE FOR RESIDUE GOL B 1702 source : AC4 32) chain B residue 426 type sequence L description BINDING SITE FOR RESIDUE GOL B 1702 source : AC4 33) chain B residue 135 type sequence R description BINDING SITE FOR RESIDUE GOL B 1703 source : AC5 34) chain B residue 141 type sequence W description BINDING SITE FOR RESIDUE GOL B 1703 source : AC5 35) chain B residue 142 type sequence K description BINDING SITE FOR RESIDUE GOL B 1703 source : AC5 36) chain A residue 419 type sequence G description BINDING SITE FOR RESIDUE GOL A 1704 source : AC6 37) chain A residue 422 type sequence H description BINDING SITE FOR RESIDUE GOL A 1704 source : AC6 38) chain A residue 423 type sequence K description BINDING SITE FOR RESIDUE GOL A 1704 source : AC6 39) chain B residue 553 type sequence R description BINDING SITE FOR RESIDUE GOL A 1704 source : AC6 40) chain A residue 268-281 type prosite sequence DWVGGRYSLWSAIG description P_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG source prosite : PS00765 41) chain A residue 359 type ACT_SITE sequence S description Proton donor => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 359 type ACT_SITE sequence S description Proton donor => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 390 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 520 type ACT_SITE sequence Q description ACT_SITE => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 390 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 520 type ACT_SITE sequence Q description ACT_SITE => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI2 47) 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 48) 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 49) 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 50) 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 51) 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 52) 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 53) 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 54) 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 55) 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 56) 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 57) 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 58) 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 59) chain A residue 3 type MOD_RES sequence A description N-acetylalanine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI4 60) chain B residue 3 type MOD_RES sequence A description N-acetylalanine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI4 61) chain A residue 13 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI5 62) chain B residue 13 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI5 63) chain A residue 87 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:Q6P6V0 source Swiss-Prot : SWS_FT_FI6 64) chain B residue 87 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:Q6P6V0 source Swiss-Prot : SWS_FT_FI6 65) chain A residue 108 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI7 66) chain B residue 108 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI7 67) chain A residue 110 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI8 68) chain B residue 110 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI8 69) chain A residue 143 type MOD_RES sequence G description N6-acetyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI9 70) chain B residue 143 type MOD_RES sequence G description N6-acetyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI9 71) chain A residue 186 type MOD_RES sequence N description Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI10 72) chain B residue 186 type MOD_RES sequence N description Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI10 73) chain A residue 251 type MOD_RES sequence A description Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0 source Swiss-Prot : SWS_FT_FI11 74) chain B residue 251 type MOD_RES sequence A description Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0 source Swiss-Prot : SWS_FT_FI11 75) chain A residue 455 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI12 76) chain B residue 455 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI12 77) chain A residue 456 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI13 78) chain B residue 456 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI13 79) chain A residue 502-519 type prosite sequence GIMWDINSFDQWGVELGK description P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GiMWdinsFDQwGVElgK source prosite : PS00174

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