eF-site ID 4ik0-AB PDB Code 4ik0 Chain A, B click to enlarge Title Crystal structure of diaminopimelate epimerase Y268A mutant from Escherichia coli Classification ISOMERASE Compound Diaminopimelate epimerase Source Escherichia coli (strain K12) (DAPF_ECOLI) Sequence A:  MQFSKMHGLGNDFMVVDAVTQNVFFSPELIRRLADRHLGV GFDQLLVVEPPYDPELDFHYRIFNADGSEVAQCGNGARCF ARFVRLKGLTNKRDIRVSTANGRMVLTVTDDDLVRVNMGE PNFEPSAVPFRANKAEKTYIMRAAEQTILCGVVSMGNPHC VIQVDDVDTAAVETLGPVLESHERFPERANIGFMQVVKRE HIRLRVYERGAGETQACGSGACAAVAVGIQQGLLAEEVRV ELPGGRLDIAWKGPGHPLYMTGPAVHVADGFIHL B:  MQFSKMHGLGNDFMVVDAVTQNVFFSPELIRRLADRHLGV GFDQLLVVEPPYDPELDFHYRIFNADGSEVAQCGNGARCF ARFVRLKGLTNKRDIRVSTANGRMVLTVTDDDLVRVNMGE PNFEPSAVPFRANKAEKTYIMRAAEQTILCGVVSMGNPHC VIQVDDVDTAAVETLGPVLESHERFPERANIGFMQVVKRE HIRLRVYERGAGETQACGSGACAAVAVGIQQGLLAEEVRV ELPGGRLDIAWKGPGHPLYMTGPAVHVADGFIHLH Description Functional site 1) chain A residue 79 type sequence C description BINDING SITE FOR RESIDUE IOD A 301 source : AC1 2) chain A residue 78 type sequence R description BINDING SITE FOR RESIDUE IOD A 303 source : AC2 3) chain A residue 171 type sequence A description BINDING SITE FOR RESIDUE IOD A 304 source : AC3 4) chain A residue 175 type sequence L description BINDING SITE FOR RESIDUE IOD A 304 source : AC3 5) chain A residue 201 type sequence H description BINDING SITE FOR RESIDUE IOD A 305 source : AC4 6) chain B residue 133 type sequence N description BINDING SITE FOR RESIDUE IOD B 302 source : AC5 7) chain B residue 11 type sequence N description BINDING SITE FOR RESIDUE IOD B 303 source : AC6 8) chain B residue 78 type sequence R description BINDING SITE FOR RESIDUE IOD B 303 source : AC6 9) chain B residue 171 type sequence A description BINDING SITE FOR RESIDUE IOD B 304 source : AC7 10) chain B residue 105 type sequence V description BINDING SITE FOR RESIDUE IOD B 305 source : AC8 11) chain B residue 201 type sequence H description BINDING SITE FOR RESIDUE IOD B 306 source : AC9 12) chain B residue 37 type sequence H description BINDING SITE FOR RESIDUE IOD B 307 source : BC1 13) chain A residue 73 type ACT_SITE sequence C description Proton donor => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 73 type ACT_SITE sequence C description Proton donor => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 217 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 217 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 11 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 18) chain B residue 44 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 19) chain B residue 64 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 20) chain B residue 74 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 21) chain B residue 157 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 190 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 208 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 218 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 44 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 64 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 74 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 157 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 190 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 208 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 218 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 32) chain B residue 11 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 159 type SITE sequence H description Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 208 type SITE sequence E description Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI4 35) chain B residue 159 type SITE sequence H description Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 208 type SITE sequence E description Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 268 type SITE sequence A description Important for dimerization => ECO:0000269|PubMed:23426375 source Swiss-Prot : SWS_FT_FI5 38) chain B residue 268 type SITE sequence A description Important for dimerization => ECO:0000269|PubMed:23426375 source Swiss-Prot : SWS_FT_FI5 39) chain A residue 64-78 type prosite sequence NADGSEVAQCGNGAR description DAP_EPIMERASE Diaminopimelate epimerase signature. NaDGSevaqCGNGaR source prosite : PS01326

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