eF-site ID 3ss4-ABCD PDB Code 3ss4 Chain A, B, C, D click to enlarge Title Crystal structure of mouse Glutaminase C, phosphate-bound form Classification HYDROLASE Compound Glutaminase C Source null (Q69ZX9_MOUSE) Sequence A:  LEDLLFYTIEKIPVHKFITALKSTGLRTSDPRLKECMDML RLTLVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFT SHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTV DGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRY VGKEPSGFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEK FDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYY LKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATL ANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAF HVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKG IHFCHDLVSLCNFHNYDNLRHFAKKLDPRR B:  LEDLLFYTIQEKIPVHKFITALKSTGLRTSDPRLKECMDM LRLTLVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSF TSHIDELYESAKKQSGGKVADYLAKFSPDLWGVSVCTVDG QRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVG KEPSGFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFD YVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLK EKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLAN GGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHV GLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIH FCHDLVSLCNFHNYDNLRHFAKKLDPRR C:  LEDLLFYTIQEKIPVHKFITALKSTGLRTSDPRLKECMDM LRLTLQTTVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDF MSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVS VCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEY VHRYVGKEPSGFLNEDDKPHNPMVNAGAIVVTSLIKQGVN NAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFA IGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVM AATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSG QFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGN SVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRR D:  LEDLLFYTIQEKIPVHKFITALKSTGLRTSDPRLKECMDM LRLTLQTTVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDF MSFTSHIDELYESAKKQSGGKVADFSPDLWGVSVCTVDGQ RHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGK EPSGFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDY VMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKE KKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANG GFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVG LPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHF CHDLVSLCNFHNYDNLRHFAKKLDPRR Description Functional site 1) chain A residue 291 type sequence S description BINDING SITE FOR RESIDUE PO4 A 1 source : AC1 2) chain A residue 340 type sequence N description BINDING SITE FOR RESIDUE PO4 A 1 source : AC1 3) chain A residue 471 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 1 source : AC1 4) chain B residue 291 type sequence S description BINDING SITE FOR RESIDUE PO4 B 2 source : AC2 5) chain B residue 340 type sequence N description BINDING SITE FOR RESIDUE PO4 B 2 source : AC2 6) chain B residue 471 type sequence Y description BINDING SITE FOR RESIDUE PO4 B 2 source : AC2 7) chain C residue 291 type sequence S description BINDING SITE FOR RESIDUE PO4 C 3 source : AC3 8) chain C residue 340 type sequence N description BINDING SITE FOR RESIDUE PO4 C 3 source : AC3 9) chain C residue 471 type sequence Y description BINDING SITE FOR RESIDUE PO4 C 3 source : AC3 10) chain D residue 291 type sequence S description BINDING SITE FOR RESIDUE PO4 D 4 source : AC4 11) chain D residue 340 type sequence N description BINDING SITE FOR RESIDUE PO4 D 4 source : AC4 12) chain D residue 392 type sequence R description BINDING SITE FOR RESIDUE PO4 D 4 source : AC4 13) chain D residue 387 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 14) chain D residue 413 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 15) chain D residue 465 type BINDING sequence M description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 16) chain D residue 483 type BINDING sequence L description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 483 type BINDING sequence L description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 18) chain C residue 285 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 19) chain C residue 334 type BINDING sequence P description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 20) chain C residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 21) chain C residue 387 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 22) chain C residue 413 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 23) chain C residue 465 type BINDING sequence M description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 24) chain C residue 483 type BINDING sequence L description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 25) chain D residue 285 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 26) chain D residue 334 type BINDING sequence P description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 27) chain D residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 483 type BINDING sequence L description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 285 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 334 type BINDING sequence P description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 285 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 334 type BINDING sequence P description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 387 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 413 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 465 type BINDING sequence M description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 387 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 39) chain B residue 413 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 465 type BINDING sequence M description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 41) chain C residue 163 type MOD_RES sequence K description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI2 42) chain D residue 163 type MOD_RES sequence K description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 163 type MOD_RES sequence K description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI2 44) chain B residue 163 type MOD_RES sequence K description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 310 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:O94925 source Swiss-Prot : SWS_FT_FI3 46) chain C residue 310 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:O94925 source Swiss-Prot : SWS_FT_FI3 47) chain D residue 310 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:O94925 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 310 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:O94925 source Swiss-Prot : SWS_FT_FI3

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