eF-site ID 2cxo-B PDB Code 2cxo Chain B click to enlarge Title Crystal structure of mouse AMF / E4P complex Classification ISOMERASE Compound Glucose-6-phosphate isomerase Source Mus musculus (Mouse) (G6PI_MOUSE) Sequence B:  MAALTRNPQFQKLLEWHRANSANLKLRELFEADPERFNNF SLNLNTNHGHILVDYSKNLVSKEVMQMLVELAKSRGVEAA RDNMFSGSKINYTEDRAVLHVALRNRSNTPIKVDGKDVMP EVNRVLDKMKSFCQRVRSGDWKGYTGKSITDIINIGIGGS DLGPLMVTEALKPYSKGGPRVWFVSNIDGTHIAKTLASLS PETSLFIIASKTFTTQETITNAETAKEWFLEAAKDPSAVA KHFVALSTNTAKVKEFGIDPQNMFEFWDWVGGRYSLWSAI GLSIALHVGFDHFEQLLSGAHWMDQHFLKTPLEKNAPVLL ALLGIWYINCYGCETHALLPYDQYMHRFAAYFQQGDMESN GKYITKSGARVDHQTGPIVWGEPGTNGQHAFYQLIHQGTK MIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMKGK LPEEARKELQAAGKSPEDLEKLLPHKVFEGNRPTNSIVFT KLTPFILGALIAMYEHKIFVQGIMWDINSFDQWGVELGKQ LAKKIEPELEGSSAVTSHDSSTNGLISFIKQQRDTKL Description Functional site 1) chain B residue 389 type sequence H description BINDING SITE FOR RESIDUE DER A 1601 source : AC1 2) chain B residue 157 type sequence I description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 3) chain B residue 158 type sequence G description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 4) chain B residue 159 type sequence G description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 5) chain B residue 160 type sequence S description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 6) chain B residue 210 type sequence S description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 7) chain B residue 211 type sequence K description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 8) chain B residue 212 type sequence T description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 9) chain B residue 215 type sequence T description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 10) chain B residue 354 type sequence Q description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 11) chain B residue 358 type sequence E description BINDING SITE FOR RESIDUE DER B 2601 source : AC2 12) chain B residue 419 type sequence G description BINDING SITE FOR RESIDUE GOL B 1702 source : AC4 13) chain B residue 423 type sequence K description BINDING SITE FOR RESIDUE GOL B 1702 source : AC4 14) chain B residue 426 type sequence L description BINDING SITE FOR RESIDUE GOL B 1702 source : AC4 15) chain B residue 135 type sequence R description BINDING SITE FOR RESIDUE GOL B 1703 source : AC5 16) chain B residue 141 type sequence W description BINDING SITE FOR RESIDUE GOL B 1703 source : AC5 17) chain B residue 142 type sequence K description BINDING SITE FOR RESIDUE GOL B 1703 source : AC5 18) chain B residue 553 type sequence R description BINDING SITE FOR RESIDUE GOL A 1704 source : AC6 19) chain B residue 359 type ACT_SITE sequence S description Proton donor => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 390 type ACT_SITE sequence A description ACT_SITE => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 520 type ACT_SITE sequence Q description ACT_SITE => ECO:0000269|PubMed:15342241 source Swiss-Prot : SWS_FT_FI2 22) 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 23) 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 24) 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 25) 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 26) 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 27) 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 28) chain B residue 3 type MOD_RES sequence A description N-acetylalanine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI4 29) chain B residue 13 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI5 30) chain B residue 87 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:Q6P6V0 source Swiss-Prot : SWS_FT_FI6 31) chain B residue 186 type MOD_RES sequence N description Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI10 32) chain B residue 251 type MOD_RES sequence A description Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0 source Swiss-Prot : SWS_FT_FI11 33) chain B residue 455 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI12 34) chain B residue 456 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI13 35) chain B residue 108 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI7 36) chain B residue 110 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI8 37) chain B residue 143 type MOD_RES sequence G description N6-acetyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI9

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