eF-site ID 1dqr-AB PDB Code 1dqr Chain A, B click to enlarge Title CRYSTAL STRUCTURE OF RABBIT PHOSPHOGLUCOSE ISOMERASE, A GLYCOLYTIC ENZYME THAT MOONLIGHTS AS NEUROLEUKIN, AUTOCRINE MOTILITY FACTOR, AND DIFFERENTIATION MEDIATOR Classification ISOMERASE Compound PHOSPHOGLUCOSE ISOMERASE Source ORGANISM_COMMON: rabbit; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus; Sequence A:  AALTRNPQFQKLQQWHREHGSELNLRHLFDTDKERFNHFS LTLNTNHGHILLDYSKNLVTEEVMHMLLDLAKSRGVEAAR ESMFNGEKINSTEDRAVLHVALRNRSNTPIVVDGKDVMPE VNKVLDKMKAFCQRVRSGDWKGYTGKTITDVINIGIGGSD LGPLMVTEALKPYSSGGPRVWFVSNIDGTHIAKTLACLNP ESSLFIIASKTFTTQETITNAKTAKDWFLLSAKDPSTVAK HFVALSTNTAKVKEFGIDPQNMFEFWDWVGGRYSLWSAIG LSIALHVGFDNFEQLLSGAHWMDQHFRTTPLEKNAPVLLA MLGIWYINCFGCETQAVLPYDQYLHRFAAYFQQGDMESNG KYITKSGARVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKM IPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMKGKS TEEARKELQAAGKSPEDLMKLLPHKVFEGNRPTNSIVFTK LTPFILGALIAMYEHKIFVQGVVWDINSFDQWGVELGKQL AKKIEPELDGSSPVTSHDSSTNGLINFIKQQREAK B:  AALTRNPQFQKLQQWHREHGSELNLRHLFDTDKERFNHFS LTLNTNHGHILLDYSKNLVTEEVMHMLLDLAKSRGVEAAR ESMFNGEKINSTEDRAVLHVALRNRSNTPIVVDGKDVMPE VNKVLDKMKAFCQRVRSGDWKGYTGKTITDVINIGIGGSD LGPLMVTEALKPYSSGGPRVWFVSNIDGTHIAKTLACLNP ESSLFIIASKTFTTQETITNAKTAKDWFLLSAKDPSTVAK HFVALSTNTAKVKEFGIDPQNMFEFWDWVGGRYSLWSAIG LSIALHVGFDNFEQLLSGAHWMDQHFRTTPLEKNAPVLLA MLGIWYINCFGCETQAVLPYDQYLHRFAAYFQQGDMESNG KYITKSGARVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKM IPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMKGKS TEEARKELQAAGKSPEDLMKLLPHKVFEGNRPTNSIVFTK LTPFILGALIAMYEHKIFVQGVVWDINSFDQWGVELGKQL AKKIEPELDGSSPVTSHDSSTNGLINFIKQQREAK Description Functional site 1) chain A residue 156 type sequence I description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 2) chain A residue 157 type sequence G description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 3) chain A residue 158 type sequence G description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 4) chain A residue 159 type sequence S description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 5) chain A residue 209 type sequence S description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 6) chain A residue 210 type sequence K description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 7) chain A residue 211 type sequence T description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 8) chain A residue 214 type sequence T description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 9) chain A residue 271 type sequence G description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 10) chain A residue 272 type sequence R description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 11) chain A residue 353 type sequence Q description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 12) chain A residue 357 type sequence E description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 13) chain A residue 511 type sequence Q description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 14) chain B residue 388 type sequence H description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 15) chain A residue 388 type sequence H description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 16) chain B residue 156 type sequence I description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 17) chain B residue 157 type sequence G description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 18) chain B residue 158 type sequence G description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 19) chain B residue 159 type sequence S description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 20) chain B residue 209 type sequence S description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 21) chain B residue 210 type sequence K description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 22) chain B residue 211 type sequence T description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 23) chain B residue 214 type sequence T description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 24) chain B residue 271 type sequence G description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 25) chain B residue 272 type sequence R description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 26) chain B residue 353 type sequence Q description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 27) chain B residue 357 type sequence E description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 28) chain A residue 210 type catalytic sequence K description 842 source MCSA : MCSA1 29) chain A residue 216 type catalytic sequence E description 842 source MCSA : MCSA1 30) chain A residue 271 type catalytic sequence G description 842 source MCSA : MCSA1 31) chain A residue 272 type catalytic sequence R description 842 source MCSA : MCSA1 32) chain A residue 357 type catalytic sequence E description 842 source MCSA : MCSA1 33) chain A residue 388 type catalytic sequence H description 842 source MCSA : MCSA1 34) chain A residue 518 type catalytic sequence K description 842 source MCSA : MCSA1 35) chain B residue 210 type catalytic sequence K description 842 source MCSA : MCSA2 36) chain B residue 216 type catalytic sequence E description 842 source MCSA : MCSA2 37) chain B residue 271 type catalytic sequence G description 842 source MCSA : MCSA2 38) chain B residue 272 type catalytic sequence R description 842 source MCSA : MCSA2 39) chain B residue 357 type catalytic sequence E description 842 source MCSA : MCSA2 40) chain B residue 388 type catalytic sequence H description 842 source MCSA : MCSA2 41) chain B residue 518 type catalytic sequence K description 842 source MCSA : MCSA2 42) chain A residue 249 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0 source Swiss-Prot : SWS_FT_FI11 43) chain B residue 249 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0 source Swiss-Prot : SWS_FT_FI11 44) chain A residue 453 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06745 source Swiss-Prot : SWS_FT_FI12 45) chain B residue 453 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06745 source Swiss-Prot : SWS_FT_FI12 46) chain A residue 501-518 type prosite sequence GVVWDINSFDQWGVELGK description P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GvVWdinsFDQwGVElgK source prosite : PS00174 47) chain A residue 267-280 type prosite sequence DWVGGRYSLWSAIG description P_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG source prosite : PS00765 48) chain A residue 357 type ACT_SITE sequence E description Proton donor => ECO:0000269|PubMed:11327814, ECO:0000269|PubMed:11425306 source Swiss-Prot : SWS_FT_FI1 49) chain B residue 357 type ACT_SITE sequence E description Proton donor => ECO:0000269|PubMed:11327814, ECO:0000269|PubMed:11425306 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 1 type MOD_RES sequence A description N-acetylalanine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI5 51) chain B residue 1 type MOD_RES sequence A description N-acetylalanine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI5 52) chain A residue 184 type MOD_RES sequence S description Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI10 53) chain B residue 184 type MOD_RES sequence S description Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI10 54) chain A residue 388 type ACT_SITE sequence H description ACT_SITE => ECO:0000269|PubMed:11327814, ECO:0000269|PubMed:11425306 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 518 type ACT_SITE sequence K description ACT_SITE => ECO:0000269|PubMed:11327814, ECO:0000269|PubMed:11425306 source Swiss-Prot : SWS_FT_FI2 56) chain B residue 388 type ACT_SITE sequence H description ACT_SITE => ECO:0000269|PubMed:11327814, ECO:0000269|PubMed:11425306 source Swiss-Prot : SWS_FT_FI2 57) chain B residue 518 type ACT_SITE sequence K description ACT_SITE => ECO:0000269|PubMed:11327814, ECO:0000269|PubMed:11425306 source Swiss-Prot : SWS_FT_FI2 58) chain A residue 11 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI6 59) chain A residue 141 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI6 60) chain B residue 11 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI6 61) chain B residue 141 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI6 62) chain A residue 33 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI7 63) chain B residue 33 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI7 64) chain A residue 106 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI8 65) chain A residue 454 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI8 66) chain B residue 106 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI8 67) chain B residue 454 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI8 68) chain A residue 108 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI9 69) chain B residue 108 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI9 70) chain A residue 158 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 71) chain B residue 388 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 72) chain A residue 209 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 73) chain A residue 353 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 74) chain A residue 357 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 75) chain A residue 388 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 76) chain B residue 158 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 77) chain B residue 209 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 78) chain B residue 353 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 79) chain B residue 357 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 80) chain A residue 518 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P06745 source Swiss-Prot : SWS_FT_FI4 81) chain B residue 518 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P06745 source Swiss-Prot : SWS_FT_FI4

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