eF-site ID 2qc8-I PDB Code 2qc8 Chain I click to enlarge Title Crystal structure of human glutamine synthetase in complex with ADP and methionine sulfoximine phosphate Classification LIGASE Compound Glutamine synthetase Source null (GLNA_HUMAN) Sequence I:  NKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDS EPKCVEELPEWNFDGSSTLQSEGSNSDMYLVPAAMFRDPF RKDPNKLVLCEVFKYNRRPAETNLRHTCKRIMDMVSNQHP WFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADR AYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGPC EGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNG AGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYD PKGGLDNARRLTGFHETSNINDFSAGVANRSASIRIPRTV GQEKKGYFEDRRPSANCDPFSVTEALIRTCLLNETG Description Functional site 1) chain I residue 136 type sequence E description BINDING SITE FOR RESIDUE MN I 401 source : CC7 2) chain I residue 196 type sequence E description BINDING SITE FOR RESIDUE MN I 401 source : CC7 3) chain I residue 203 type sequence E description BINDING SITE FOR RESIDUE MN I 401 source : CC7 4) chain I residue 134 type sequence E description BINDING SITE FOR RESIDUE MN I 402 source : CC8 5) chain I residue 253 type sequence H description BINDING SITE FOR RESIDUE MN I 402 source : CC8 6) chain I residue 338 type sequence E description BINDING SITE FOR RESIDUE MN I 402 source : CC8 7) chain I residue 340 type sequence R description BINDING SITE FOR RESIDUE MN I 402 source : CC8 8) chain I residue 134 type sequence E description BINDING SITE FOR RESIDUE MN I 403 source : CC9 9) chain I residue 203 type sequence E description BINDING SITE FOR RESIDUE MN I 403 source : CC9 10) chain I residue 193 type sequence T description BINDING SITE FOR RESIDUE CL I 709 source : EC3 11) chain I residue 44 type sequence T description BINDING SITE FOR RESIDUE CL J 710 source : EC4 12) chain I residue 130 type sequence W description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 13) chain I residue 132 type sequence G description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 14) chain I residue 134 type sequence E description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 15) chain I residue 203 type sequence E description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 16) chain I residue 205 type sequence Q description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 17) chain I residue 206 type sequence I description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 18) chain I residue 207 type sequence G description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 19) chain I residue 208 type sequence P description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 20) chain I residue 255 type sequence N description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 21) chain I residue 257 type sequence S description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 22) chain I residue 319 type sequence R description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 23) chain I residue 324 type sequence R description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 24) chain I residue 336 type sequence Y description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 25) chain I residue 338 type sequence E description BINDING SITE FOR RESIDUE ADP I 501 source : GC3 26) chain I residue 134 type sequence E description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 27) chain I residue 136 type sequence E description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 28) chain I residue 196 type sequence E description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 29) chain I residue 203 type sequence E description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 30) chain I residue 248 type sequence N description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 31) chain I residue 249 type sequence G description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 32) chain I residue 251 type sequence G description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 33) chain I residue 253 type sequence H description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 34) chain I residue 299 type sequence R description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 35) chain I residue 305 type sequence E description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 36) chain I residue 319 type sequence R description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 37) chain I residue 324 type sequence R description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 38) chain I residue 338 type sequence E description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 39) chain I residue 340 type sequence R description BINDING SITE FOR RESIDUE P3S I 601 source : GC4 40) chain I residue 63 type sequence D description BINDING SITE FOR RESIDUE P3S J 601 source : GC6 41) chain I residue 134 type BINDING sequence E description BINDING => ECO:0007744|PDB:2QC8 source Swiss-Prot : SWS_FT_FI1 42) chain I residue 136 type BINDING sequence E description BINDING => ECO:0007744|PDB:2QC8 source Swiss-Prot : SWS_FT_FI1 43) chain I residue 196 type BINDING sequence E description BINDING => ECO:0007744|PDB:2QC8 source Swiss-Prot : SWS_FT_FI1 44) chain I residue 203 type BINDING sequence E description BINDING => ECO:0007744|PDB:2QC8 source Swiss-Prot : SWS_FT_FI1 45) chain I residue 253 type BINDING sequence H description BINDING => ECO:0007744|PDB:2QC8 source Swiss-Prot : SWS_FT_FI1 46) chain I residue 338 type BINDING sequence E description BINDING => ECO:0007744|PDB:2QC8 source Swiss-Prot : SWS_FT_FI1 47) chain I residue 246 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P9WN39 source Swiss-Prot : SWS_FT_FI2 48) chain I residue 319 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WN39 source Swiss-Prot : SWS_FT_FI2 49) chain I residue 340 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WN39 source Swiss-Prot : SWS_FT_FI2 50) chain I residue 255 type BINDING sequence N description BINDING => ECO:0007744|PDB:2OJW, ECO:0007744|PDB:2QC8 source Swiss-Prot : SWS_FT_FI3 51) chain I residue 324 type BINDING sequence R description BINDING => ECO:0007744|PDB:2OJW, ECO:0007744|PDB:2QC8 source Swiss-Prot : SWS_FT_FI3 52) chain I residue 336 type BINDING sequence Y description BINDING => ECO:0007744|PDB:2OJW, ECO:0007744|PDB:2QC8 source Swiss-Prot : SWS_FT_FI3 53) chain I residue 104 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P15105 source Swiss-Prot : SWS_FT_FI4 54) chain I residue 343 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5

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