eF-site ID 3ss3-ABCD PDB Code 3ss3 Chain A, B, C, D click to enlarge Title Crystal structure of mouse Glutaminase C, ligand-free form Classification HYDROLASE Compound Glutaminase C Source null (Q69ZX9_MOUSE) Sequence A:  LEDLLFYTIQEKIPVHKFITALKSTGLRTSDPRLKECMDM LRLTLQTTVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDF MSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVS VCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEY VHRYVGKEPSGFLNEDDKPHNPMVNAGAIVVTSLIKQGVN NAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFA IGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVM AATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSG QFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGN SVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRR B:  LEDLLFYTIAQEKIPVHKFITALKSTGLRTSDPRLKECMD MLRLTLQTTMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDF MSFTSHIDELYESAKKQSGGKVAQLAKFSPDLWGVSVCTV DGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRY VGKEPSLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEK FDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYY LKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATL ANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAF HVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKG IHFCHDLVSLCNFHNYDNLRHFAKKLDPRR C:  LEDLLFYTIQEKIPVHKFITALKSTGLRTSDPRLKECMDM LRLTMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTS HIDELYESAKKQSGGKVADKFSPDLWGVSVCTVDGQRHSI GDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSG FLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQF LNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCF PEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCP ITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK SGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDL VSLCNFHNYDNLRHFAKKLDPRR D:  LEDLLFYTIQEKIPVHKFITALKSTGLRTSDPRLKECMDM LRLTVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFT SHIDELYESAKKQSGGKVQLAKFSPDLWGVSVCTVDGQRH SIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEP SFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQ FLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKC FPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFC PITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPA KSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHD LVSLCNFHNYDNLRHFAKKLDPRRE Description Functional site 1) chain A residue 290 type sequence Q description BINDING SITE FOR RESIDUE CL A 1 source : AC1 2) chain A residue 291 type sequence S description BINDING SITE FOR RESIDUE CL A 1 source : AC1 3) chain A residue 471 type sequence Y description BINDING SITE FOR RESIDUE CL A 1 source : AC1 4) chain A residue 489 type sequence V description BINDING SITE FOR RESIDUE CL A 1 source : AC1 5) chain B residue 291 type sequence S description BINDING SITE FOR RESIDUE CL B 2 source : AC2 6) chain B residue 471 type sequence Y description BINDING SITE FOR RESIDUE CL B 2 source : AC2 7) chain B residue 489 type sequence V description BINDING SITE FOR RESIDUE CL B 2 source : AC2 8) chain C residue 290 type sequence Q description BINDING SITE FOR RESIDUE CL C 3 source : AC3 9) chain C residue 291 type sequence S description BINDING SITE FOR RESIDUE CL C 3 source : AC3 10) chain C residue 471 type sequence Y description BINDING SITE FOR RESIDUE CL C 3 source : AC3 11) chain C residue 489 type sequence V description BINDING SITE FOR RESIDUE CL C 3 source : AC3 12) chain D residue 291 type sequence S description BINDING SITE FOR RESIDUE CL D 4 source : AC4 13) chain D residue 471 type sequence Y description BINDING SITE FOR RESIDUE CL D 4 source : AC4 14) chain D residue 489 type sequence V description BINDING SITE FOR RESIDUE CL D 4 source : AC4 15) chain D residue 387 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 16) chain D residue 413 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 17) chain D residue 465 type BINDING sequence M description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 18) chain D residue 483 type BINDING sequence L description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 285 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 334 type BINDING sequence P description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 387 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 413 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 465 type BINDING sequence M description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 483 type BINDING sequence L description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 285 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 334 type BINDING sequence P description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 387 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 413 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 465 type BINDING sequence M description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 483 type BINDING sequence L description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 33) chain C residue 285 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 34) chain C residue 334 type BINDING sequence P description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 35) chain C residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 36) chain C residue 387 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 37) chain C residue 413 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 38) chain C residue 465 type BINDING sequence M description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 39) chain C residue 483 type BINDING sequence L description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 40) chain D residue 285 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 41) chain D residue 334 type BINDING sequence P description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 42) chain D residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5 source Swiss-Prot : SWS_FT_FI1 43) chain C residue 163 type MOD_RES sequence K description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI2 44) chain D residue 163 type MOD_RES sequence K description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 163 type MOD_RES sequence K description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 163 type MOD_RES sequence K description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 310 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:O94925 source Swiss-Prot : SWS_FT_FI3 48) chain B residue 310 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:O94925 source Swiss-Prot : SWS_FT_FI3 49) chain C residue 310 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:O94925 source Swiss-Prot : SWS_FT_FI3 50) chain D residue 310 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:O94925 source Swiss-Prot : SWS_FT_FI3

Display surface Download Links