eF-site ID 1dqr-B PDB Code 1dqr Chain 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 B:  AALTRNPQFQKLQQWHREHGSELNLRHLFDTDKERFNHFS LTLNTNHGHILLDYSKNLVTEEVMHMLLDLAKSRGVEAAR ESMFNGEKINSTEDRAVLHVALRNRSNTPIVVDGKDVMPE VNKVLDKMKAFCQRVRSGDWKGYTGKTITDVINIGIGGSD LGPLMVTEALKPYSSGGPRVWFVSNIDGTHIAKTLACLNP ESSLFIIASKTFTTQETITNAKTAKDWFLLSAKDPSTVAK HFVALSTNTAKVKEFGIDPQNMFEFWDWVGGRYSLWSAIG LSIALHVGFDNFEQLLSGAHWMDQHFRTTPLEKNAPVLLA MLGIWYINCFGCETQAVLPYDQYLHRFAAYFQQGDMESNG KYITKSGARVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKM IPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMKGKS TEEARKELQAAGKSPEDLMKLLPHKVFEGNRPTNSIVFTK LTPFILGALIAMYEHKIFVQGVVWDINSFDQWGVELGKQL AKKIEPELDGSSPVTSHDSSTNGLINFIKQQREAK Description Functional site 1) chain B residue 388 type sequence H description BINDING SITE FOR RESIDUE 6PG A 600 source : AC1 2) chain B residue 156 type sequence I description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 3) chain B residue 157 type sequence G description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 4) chain B residue 158 type sequence G description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 5) chain B residue 159 type sequence S description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 6) chain B residue 209 type sequence S description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 7) chain B residue 210 type sequence K description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 8) chain B residue 211 type sequence T description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 9) chain B residue 214 type sequence T description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 10) chain B residue 271 type sequence G description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 11) chain B residue 272 type sequence R description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 12) chain B residue 353 type sequence Q description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 13) chain B residue 357 type sequence E description BINDING SITE FOR RESIDUE 6PG B 601 source : AC2 14) chain B residue 210 type catalytic sequence K description 842 source MCSA : MCSA2 15) chain B residue 216 type catalytic sequence E description 842 source MCSA : MCSA2 16) chain B residue 271 type catalytic sequence G description 842 source MCSA : MCSA2 17) chain B residue 272 type catalytic sequence R description 842 source MCSA : MCSA2 18) chain B residue 357 type catalytic sequence E description 842 source MCSA : MCSA2 19) chain B residue 388 type catalytic sequence H description 842 source MCSA : MCSA2 20) chain B residue 518 type catalytic sequence K description 842 source MCSA : MCSA2 21) chain B residue 249 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0 source Swiss-Prot : SWS_FT_FI11 22) chain B residue 453 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06745 source Swiss-Prot : SWS_FT_FI12 23) 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 24) 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 25) 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 26) chain B residue 158 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 27) chain B residue 388 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 28) chain B residue 209 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 29) chain B residue 353 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 30) chain B residue 357 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX source Swiss-Prot : SWS_FT_FI3 31) chain B residue 518 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P06745 source Swiss-Prot : SWS_FT_FI4 32) chain B residue 1 type MOD_RES sequence A description N-acetylalanine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI5 33) chain B residue 11 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI6 34) chain B residue 141 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI6 35) chain B residue 33 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI7 36) chain B residue 106 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI8 37) chain B residue 454 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI8 38) chain B residue 108 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI9 39) chain B residue 184 type MOD_RES sequence S description Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P06744 source Swiss-Prot : SWS_FT_FI10

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