eF-site ID 1dpp-ACEG PDB Code 1dpp Chain A, C, E, G click to enlarge Title DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE Classification PEPTIDE BINDING PROTEIN Compound DIPEPTIDE BINDING PROTEIN Source ORGANISM_SCIENTIFIC: Escherichia coli; Sequence A:  KTLVYCSEGSPEGFNPQLFTSGTTYDASSVPLYNRLVEFK IGTTEVIPGLAEKWEVSEDGKTYTFHLRKGVKWHDNKEFK PTRELNADDVVFSFDRQKNAQNPYHKVSGGSYEYFEGMGL PELISEVKKVDDNTVQFVLTRPEAPFLADLAMDFASILSK EYADAMMKAGTPEKLDLNPIGTGPFQLQQYQKDSRIRYKA FDGYWGTKPQIDTLVFSITPDASVRYAKLQKNECQVMPYP NPADIARMKQDKSINLMEMPGLNVGYLSYNVQKKPLDDVK VRQALTYAVNKDAIIKAVYQGAGVSAKNLIPPTMWGYNDD VQDYTYDPEKAKALLKEAGLEKGFSIDLWAMPVQRPYNPN ARRMAEMIQADWAKVGVQAKIVTYEWGEYLKRAKDGEHQT VMMGWTGDNGDPDNFFATLFSCAASEQGSNYSKWCYKPFE DLIQPARATDDHNKRVELYKQAQVVMHDQAPALIIAHSTV FEPVRKEVKGYVVDPLGKHHFENVSIE C:  KTLVYCSEGSPEGFNPQLFTSGTTYDASSVPLYNRLVEFK IGTTEVIPGLAEKWEVSEDGKTYTFHLRKGVKWHDNKEFK PTRELNADDVVFSFDRQKNAQNPYHKVSGGSYEYFEGMGL PELISEVKKVDDNTVQFVLTRPEAPFLADLAMDFASILSK EYADAMMKAGTPEKLDLNPIGTGPFQLQQYQKDSRIRYKA FDGYWGTKPQIDTLVFSITPDASVRYAKLQKNECQVMPYP NPADIARMKQDKSINLMEMPGLNVGYLSYNVQKKPLDDVK VRQALTYAVNKDAIIKAVYQGAGVSAKNLIPPTMWGYNDD VQDYTYDPEKAKALLKEAGLEKGFSIDLWAMPVQRPYNPN ARRMAEMIQADWAKVGVQAKIVTYEWGEYLKRAKDGEHQT VMMGWTGDNGDPDNFFATLFSCAASEQGSNYSKWCYKPFE DLIQPARATDDHNKRVELYKQAQVVMHDQAPALIIAHSTV FEPVRKEVKGYVVDPLGKHHFENVSIE E:  KTLVYCSEGSPEGFNPQLFTSGTTYDASSVPLYNRLVEFK IGTTEVIPGLAEKWEVSEDGKTYTFHLRKGVKWHDNKEFK PTRELNADDVVFSFDRQKNAQNPYHKVSGGSYEYFEGMGL PELISEVKKVDDNTVQFVLTRPEAPFLADLAMDFASILSK EYADAMMKAGTPEKLDLNPIGTGPFQLQQYQKDSRIRYKA FDGYWGTKPQIDTLVFSITPDASVRYAKLQKNECQVMPYP NPADIARMKQDKSINLMEMPGLNVGYLSYNVQKKPLDDVK VRQALTYAVNKDAIIKAVYQGAGVSAKNLIPPTMWGYNDD VQDYTYDPEKAKALLKEAGLEKGFSIDLWAMPVQRPYNPN ARRMAEMIQADWAKVGVQAKIVTYEWGEYLKRAKDGEHQT VMMGWTGDNGDPDNFFATLFSCAASEQGSNYSKWCYKPFE DLIQPARATDDHNKRVELYKQAQVVMHDQAPALIIAHSTV FEPVRKEVKGYVVDPLGKHHFENVSIE G:  KTLVYCSEGSPEGFNPQLFTSGTTYDASSVPLYNRLVEFK IGTTEVIPGLAEKWEVSEDGKTYTFHLRKGVKWHDNKEFK PTRELNADDVVFSFDRQKNAQNPYHKVSGGSYEYFEGMGL PELISEVKKVDDNTVQFVLTRPEAPFLADLAMDFASILSK EYADAMMKAGTPEKLDLNPIGTGPFQLQQYQKDSRIRYKA FDGYWGTKPQIDTLVFSITPDASVRYAKLQKNECQVMPYP NPADIARMKQDKSINLMEMPGLNVGYLSYNVQKKPLDDVK VRQALTYAVNKDAIIKAVYQGAGVSAKNLIPPTMWGYNDD VQDYTYDPEKAKALLKEAGLEKGFSIDLWAMPVQRPYNPN ARRMAEMIQADWAKVGVQAKIVTYEWGEYLKRAKDGEHQT VMMGWTGDNGDPDNFFATLFSCAASEQGSNYSKWCYKPFE DLIQPARATDDHNKRVELYKQAQVVMHDQAPALIIAHSTV FEPVRKEVKGYVVDPLGKHHFENVSIE Description (1)  DIPEPTIDE BINDING PROTEIN, GLYCYL-L-LEUCINE Functional site 1) chain A residue 20 type sequence T description BINDING SITE FOR RESIDUE GLY A 1001 source : AC1 2) chain A residue 114 type sequence Y description BINDING SITE FOR RESIDUE GLY A 1001 source : AC1 3) chain A residue 405 type sequence W description BINDING SITE FOR RESIDUE GLY A 1001 source : AC1 4) chain A residue 406 type sequence T description BINDING SITE FOR RESIDUE GLY A 1001 source : AC1 5) chain A residue 408 type sequence D description BINDING SITE FOR RESIDUE GLY A 1001 source : AC1 6) chain A residue 20 type sequence T description BINDING SITE FOR RESIDUE LEU A 1002 source : AC2 7) chain A residue 21 type sequence S description BINDING SITE FOR RESIDUE LEU A 1002 source : AC2 8) chain A residue 22 type sequence G description BINDING SITE FOR RESIDUE LEU A 1002 source : AC2 9) chain A residue 355 type sequence R description BINDING SITE FOR RESIDUE LEU A 1002 source : AC2 10) chain A residue 357 type sequence Y description BINDING SITE FOR RESIDUE LEU A 1002 source : AC2 11) chain A residue 403 type sequence M description BINDING SITE FOR RESIDUE LEU A 1002 source : AC2 12) chain A residue 404 type sequence G description BINDING SITE FOR RESIDUE LEU A 1002 source : AC2 13) chain C residue 20 type sequence T description BINDING SITE FOR RESIDUE GLY C 1001 source : AC3 14) chain C residue 114 type sequence Y description BINDING SITE FOR RESIDUE GLY C 1001 source : AC3 15) chain C residue 405 type sequence W description BINDING SITE FOR RESIDUE GLY C 1001 source : AC3 16) chain C residue 406 type sequence T description BINDING SITE FOR RESIDUE GLY C 1001 source : AC3 17) chain C residue 408 type sequence D description BINDING SITE FOR RESIDUE GLY C 1001 source : AC3 18) chain C residue 20 type sequence T description BINDING SITE FOR RESIDUE LEU C 1002 source : AC4 19) chain C residue 21 type sequence S description BINDING SITE FOR RESIDUE LEU C 1002 source : AC4 20) chain C residue 22 type sequence G description BINDING SITE FOR RESIDUE LEU C 1002 source : AC4 21) chain C residue 355 type sequence R description BINDING SITE FOR RESIDUE LEU C 1002 source : AC4 22) chain C residue 357 type sequence Y description BINDING SITE FOR RESIDUE LEU C 1002 source : AC4 23) chain C residue 403 type sequence M description BINDING SITE FOR RESIDUE LEU C 1002 source : AC4 24) chain C residue 404 type sequence G description BINDING SITE FOR RESIDUE LEU C 1002 source : AC4 25) chain E residue 20 type sequence T description BINDING SITE FOR RESIDUE GLY E 1001 source : AC5 26) chain E residue 114 type sequence Y description BINDING SITE FOR RESIDUE GLY E 1001 source : AC5 27) chain E residue 405 type sequence W description BINDING SITE FOR RESIDUE GLY E 1001 source : AC5 28) chain E residue 406 type sequence T description BINDING SITE FOR RESIDUE GLY E 1001 source : AC5 29) chain E residue 408 type sequence D description BINDING SITE FOR RESIDUE GLY E 1001 source : AC5 30) chain E residue 20 type sequence T description BINDING SITE FOR RESIDUE LEU E 1002 source : AC6 31) chain E residue 21 type sequence S description BINDING SITE FOR RESIDUE LEU E 1002 source : AC6 32) chain E residue 22 type sequence G description BINDING SITE FOR RESIDUE LEU E 1002 source : AC6 33) chain E residue 355 type sequence R description BINDING SITE FOR RESIDUE LEU E 1002 source : AC6 34) chain E residue 357 type sequence Y description BINDING SITE FOR RESIDUE LEU E 1002 source : AC6 35) chain E residue 403 type sequence M description BINDING SITE FOR RESIDUE LEU E 1002 source : AC6 36) chain E residue 404 type sequence G description BINDING SITE FOR RESIDUE LEU E 1002 source : AC6 37) chain G residue 20 type sequence T description BINDING SITE FOR RESIDUE GLY G 1001 source : AC7 38) chain G residue 114 type sequence Y description BINDING SITE FOR RESIDUE GLY G 1001 source : AC7 39) chain G residue 405 type sequence W description BINDING SITE FOR RESIDUE GLY G 1001 source : AC7 40) chain G residue 406 type sequence T description BINDING SITE FOR RESIDUE GLY G 1001 source : AC7 41) chain G residue 408 type sequence D description BINDING SITE FOR RESIDUE GLY G 1001 source : AC7 42) chain G residue 20 type sequence T description BINDING SITE FOR RESIDUE LEU G 1002 source : AC8 43) chain G residue 21 type sequence S description BINDING SITE FOR RESIDUE LEU G 1002 source : AC8 44) chain G residue 22 type sequence G description BINDING SITE FOR RESIDUE LEU G 1002 source : AC8 45) chain G residue 355 type sequence R description BINDING SITE FOR RESIDUE LEU G 1002 source : AC8 46) chain G residue 357 type sequence Y description BINDING SITE FOR RESIDUE LEU G 1002 source : AC8 47) chain G residue 403 type sequence M description BINDING SITE FOR RESIDUE LEU G 1002 source : AC8 48) chain G residue 404 type sequence G description BINDING SITE FOR RESIDUE LEU G 1002 source : AC8 49) chain A residue 51-73 type prosite sequence AEKWEVSEDGKTYTFHLRKGVKW description SBP_BACTERIAL_5 Bacterial extracellular solute-binding proteins, family 5 signature. AekwevseDgkTYtFhLRKGVKW source prosite : PS01040 50) chain A residue 20 type BINDING sequence T description BINDING => ECO:0000269|PubMed:8563629, ECO:0007744|PDB:1DPP source Swiss-Prot : SWS_FT_FI1 51) chain G residue 20 type BINDING sequence T description BINDING => ECO:0000269|PubMed:8563629, ECO:0007744|PDB:1DPP source Swiss-Prot : SWS_FT_FI1 52) chain G residue 355 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8563629, ECO:0007744|PDB:1DPP source Swiss-Prot : SWS_FT_FI1 53) chain G residue 405 type BINDING sequence W description BINDING => ECO:0000269|PubMed:8563629, ECO:0007744|PDB:1DPP source Swiss-Prot : SWS_FT_FI1 54) chain A residue 355 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8563629, ECO:0007744|PDB:1DPP source Swiss-Prot : SWS_FT_FI1 55) chain A residue 405 type BINDING sequence W description BINDING => ECO:0000269|PubMed:8563629, ECO:0007744|PDB:1DPP source Swiss-Prot : SWS_FT_FI1 56) chain C residue 20 type BINDING sequence T description BINDING => ECO:0000269|PubMed:8563629, ECO:0007744|PDB:1DPP source Swiss-Prot : SWS_FT_FI1 57) chain C residue 355 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8563629, ECO:0007744|PDB:1DPP source Swiss-Prot : SWS_FT_FI1 58) chain C residue 405 type BINDING sequence W description BINDING => ECO:0000269|PubMed:8563629, ECO:0007744|PDB:1DPP source Swiss-Prot : SWS_FT_FI1 59) chain E residue 20 type BINDING sequence T description BINDING => ECO:0000269|PubMed:8563629, ECO:0007744|PDB:1DPP source Swiss-Prot : SWS_FT_FI1 60) chain E residue 355 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8563629, ECO:0007744|PDB:1DPP source Swiss-Prot : SWS_FT_FI1 61) chain E residue 405 type BINDING sequence W description BINDING => ECO:0000269|PubMed:8563629, ECO:0007744|PDB:1DPP source Swiss-Prot : SWS_FT_FI1

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