eF-site ID 2yfh-ABCDEF PDB Code 2yfh Chain A, B, C, D, E, F click to enlarge Title Structure of a Chimeric Glutamate Dehydrogenase Classification OXIDOREDUCTASE Compound GLUTAMATE DEHYDROGENASE, NAD-SPECIFIC GLUTAMATE DEHYDROGENASE, GLUTAMATE DEHYDROGENASE Source [Clostridium] symbiosum WAL-14163 (DHE4_ECOLI) Sequence A:  MSKYVDRVIAEVEKKYADEPEFVQTVEEVLSSLGPVVDAH PEYEEVALLERMVIPERVIEFRVPWEDDNGKVHVNTGYRV QFNGAIGPYKGGLRFAPSVNLSIMKFLGFEQAFKDSLTTL PMGGAKGGSDFDPNGKSDREVMRFCQAFMTELYRHIGPDI DVPAGDLGVGAREIGYMYGQYRKIVGGFYNGVLTGKARSF GGSLIRPEATGYGLVYFTEAMLKRHGMGFEGMRVSVSGSG NVAQYAIEKAMEFGARVITASDSSGTVVDESGFTKEKLAR LIEIDGRVADYAKEFGLVYLEGQQPWSLPVDIALPCATQN ELDVDAAHQLIANGVKAVAEGANMPTTIEATELFQQAGVL FAPGKAANAGGVATSGLEMAQNAARLGWKAEKVDARLHHI MTDIHDGSAAAAERYGLGYNLVAGANIVGFQKIADAMMAQ GIAW B:  SKYVDRVIAEVEKKYADEPEFVQTVEEVLSSLGPVVDAHP EYEEVALLERMVIPERVIEFRVPWEDDNGKVHVNTGYRVQ FNGAIGPYKGGLRFAPSVNLSIMKFLGFEQAFKDSLTTLP MGGAKGGSDFDPNGKSDREVMRFCQAFMTELYRHIGPDID VPAGDLGVGAREIGYMYGQYRKIVGGFYNGVLTGKARSFG GSLIRPEATGYGLVYFTEAMLKRHGMGFEGMRVSVSGSGN VAQYAIEKAMEFGARVITASDSSGTVVDESGFTKEKLARL IEIKASRDGRVADYAKEFGLVYLEGQQPWSLPVDIALPCA TQNELDVDAAHQLIANGVKAVAEGANMPTTIEATELFQQA GVLFAPGKAANAGGVATSGLEMAQNAARLGWKAEKVDARL HHIMTDIHDGSAAAAERYGLGYNLVAGANIVGFQKIADAM MAQGIAW C:  SKYVDRVIAEVEKKYADEPEFVQTVEEVLSSLGPVVDAHP EYEEVALLERMVIPERVIEFRVPWEDDNGKVHVNTGYRVQ FNGAIGPYKGGLRFAPSVNLSIMKFLGFEQAFKDSLTTLP MGGAKGGSDFDPNGKSDREVMRFCQAFMTELYRHIGPDID VPAGDLGVGAREIGYMYGQYRKIVGGFYNGVLTGKARSFG GSLIRPEATGYGLVYFTEAMLKRHGMGFEGMRVSVSGSGN VAQYAIEKAMEFGARVITASDSSGTVVDESGFTKEKLARL IEIKASRDGRVADYAKEFGLVYLEGQQPWSLPVDIALPCA TQNELDVDAAHQLIANGVKAVAEGANMPTTIEATELFQQA GVLFAPGKAANAGGVATSGLEMAQNAARLGWKAEKVDARL HHIMTDIHDGSAAAAERYGLGYNLVAGANIVGFQKIADAM MAQGIAW D:  SKYVDRVIAEVEKKYADEPEFVQTVEEVLSSLGPVVDAHP EYEEVALLERMVIPERVIEFRVPWEDDNGKVHVNTGYRVQ FNGAIGPYKGGLRFAPSVNLSIMKFLGFEQAFKDSLTTLP MGGAKGGSDFDPNGKSDREVMRFCQAFMTELYRHIGPDID VPAGDLGVGAREIGYMYGQYRKIVGGFYNGVLTGKARSFG GSLIRPEATGYGLVYFTEAMLKRHGMGFEGMRVSVSGSGN VAQYAIEKAMEFGARVITASDSSGTVVDESGFTKEKLARL IEIKAGRVADYAKEFGLVYLEGQQPWSLPVDIALPCATQN ELDVDAAHQLIANGVKAVAEGANMPTTIEATELFQQAGVL FAPGKAANAGGVATSGLEMAQNAARLGWKAEKVDARLHHI MTDIHDGSAAAAERYGLGYNLVAGANIVGFQKIADAMMAQ GIAW E:  MSKYVDRVIAEVEKKYADEPEFVQTVEEVLSSLGPVVDAH PEYEEVALLERMVIPERVIEFRVPWEDDNGKVHVNTGYRV QFNGAIGPYKGGLRFAPSVNLSIMKFLGFEQAFKDSLTTL PMGGAKGGSDFDPNGKSDREVMRFCQAFMTELYRHIGPDI DVPAGDLGVGAREIGYMYGQYRKIVGGFYNGVLTGKARSF GGSLIRPEATGYGLVYFTEAMLKRHGMGFEGMRVSVSGSG NVAQYAIEKAMEFGARVITASDSSGTVVDESGFTKEKLAR LIEIKASRDGRVADYAKEFGLVYLEGQQPWSLPVDIALPC ATQNELDVDAAHQLIANGVKAVAEGANMPTTIEATELFQQ AGVLFAPGKAANAGGVATSGLEMAQNAARLGWKAEKVDAR LHHIMTDIHDGSAAAAERYGLGYNLVAGANIVGFQKIADA MMAQGIAW F:  SKYVDRVIAEVEKKYADEPEFVQTVEEVLSSLGPVVDAHP EYEEVALLERMVIPERVIEFRVPWEDDNGKVHVNTGYRVQ FNGAIGPYKGGLRFAPSVNLSIMKFLGFEQAFKDSLTTLP MGGAKGGSDFDPNGKSDREVMRFCQAFMTELYRHIGPDID VPAGDLGVGAREIGYMYGQYRKIVGGFYNGVLTGKARSFG GSLIRPEATGYGLVYFTEAMLKRHGMGFEGMRVSVSGSGN VAQYAIEKAMEFGARVITASDSSGTVVDESGFTKEKLARL IEIKASRDGRVADYAKEFGLVYLEGQQPWSLPVDIALPCA TQNELDVDAAHQLIANGVKAVAEGANMPTTIEATELFQQA GVLFAPGKAANAGGVATSGLEMAQNAARLGWKAEKVDARL HHIMTDIHDGSAAAAERYGLGYNLVAGANIVGFQKIADAM MAQGIAW Description Functional site 1) chain A residue 120-133 type prosite sequence LPMGGAKGGSDFDP description GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LpmGGAKgGsdfDP source prosite : PS00074 2) chain A residue 210 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 3) chain D residue 210 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 4) chain D residue 241 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 5) chain D residue 379 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 6) chain E residue 210 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 7) chain E residue 241 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 8) chain E residue 379 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 9) chain F residue 210 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 10) chain F residue 241 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 11) chain F residue 379 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 241 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 379 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 210 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 241 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 16) chain B residue 379 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 17) chain C residue 210 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 18) chain C residue 241 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 19) chain C residue 379 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1

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