eF-site ID 1te6-B PDB Code 1te6 Chain B click to enlarge Title Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom Classification LYASE Compound Gamma enolase Source Homo sapiens (Human) (ENOG_HUMAN) Sequence B:  SIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGAST GIYEALELRDGDKQRYLGKGVLKAVDHINSTIAPALISSG LSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKA GAAERELPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGN KLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYG KDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKIV IGMDVAASEFYRDGKYDLDFKSPTDPSRYITGDQLGALYQ DFVRDYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLT VTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQ ENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS ERLAKYNQLMRIEEELGDEARFAGHNFRNPSVL Description Functional site 1) chain B residue 244 type sequence D description BINDING SITE FOR RESIDUE MG B 740 source : AC4 2) chain B residue 292 type sequence E description BINDING SITE FOR RESIDUE MG B 740 source : AC4 3) chain B residue 317 type sequence D description BINDING SITE FOR RESIDUE MG B 740 source : AC4 4) chain B residue 342 type sequence K description BINDING SITE FOR RESIDUE CL B 742 source : AC5 5) chain B residue 371 type sequence R description BINDING SITE FOR RESIDUE CL B 742 source : AC5 6) chain B residue 372 type sequence S description BINDING SITE FOR RESIDUE CL B 742 source : AC5 7) chain B residue 210 type ACT_SITE sequence G description Proton donor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI1 8) chain B residue 343 type ACT_SITE sequence V description Proton acceptor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI2 9) chain B residue 318 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 10) chain B residue 370 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 11) chain B residue 394 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 12) chain B residue 158 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 13) chain B residue 167 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 14) chain B residue 293 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 15) chain B residue 245 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI5 16) chain B residue 263 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 17) chain B residue 287 type MOD_RES sequence P description Phosphotyrosine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI15 18) chain B residue 291 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI16 19) chain B residue 335 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 20) chain B residue 343 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 21) chain B residue 406 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 22) chain B residue 202 type CROSSLNK sequence D description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI18 23) chain B residue 2 type MOD_RES sequence I description N-acetylserine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI6 24) chain B residue 5 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 25) chain B residue 64 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 26) chain B residue 193 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 27) chain B residue 256 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 28) chain B residue 26 type MOD_RES sequence A description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI8 29) chain B residue 44 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI9 30) chain B residue 40 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI3 31) chain B residue 60 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 32) chain B residue 89 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 33) chain B residue 228 type MOD_RES sequence E description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 34) chain B residue 197 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:P17183 source Swiss-Prot : SWS_FT_FI11 35) chain B residue 199 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P17183 source Swiss-Prot : SWS_FT_FI11 36) chain B residue 202 type MOD_RES sequence D description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI12 37) chain B residue 233 type MOD_RES sequence A description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI13

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