eF-site ID 4ik0-B PDB Code 4ik0 Chain 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 B:  MQFSKMHGLGNDFMVVDAVTQNVFFSPELIRRLADRHLGV GFDQLLVVEPPYDPELDFHYRIFNADGSEVAQCGNGARCF ARFVRLKGLTNKRDIRVSTANGRMVLTVTDDDLVRVNMGE PNFEPSAVPFRANKAEKTYIMRAAEQTILCGVVSMGNPHC VIQVDDVDTAAVETLGPVLESHERFPERANIGFMQVVKRE HIRLRVYERGAGETQACGSGACAAVAVGIQQGLLAEEVRV ELPGGRLDIAWKGPGHPLYMTGPAVHVADGFIHLH Description Functional site 1) chain B residue 133 type sequence N description BINDING SITE FOR RESIDUE IOD B 302 source : AC5 2) chain B residue 11 type sequence N description BINDING SITE FOR RESIDUE IOD B 303 source : AC6 3) chain B residue 78 type sequence R description BINDING SITE FOR RESIDUE IOD B 303 source : AC6 4) chain B residue 171 type sequence A description BINDING SITE FOR RESIDUE IOD B 304 source : AC7 5) chain B residue 105 type sequence V description BINDING SITE FOR RESIDUE IOD B 305 source : AC8 6) chain B residue 201 type sequence H description BINDING SITE FOR RESIDUE IOD B 306 source : AC9 7) chain B residue 37 type sequence H description BINDING SITE FOR RESIDUE IOD B 307 source : BC1 8) chain B residue 73 type ACT_SITE sequence C description Proton donor => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI1 9) chain B residue 217 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI2 10) chain B residue 64 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 11) chain B residue 74 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 12) chain B residue 157 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 190 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 14) chain B residue 208 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 15) chain B residue 218 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 44 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 17) chain B residue 11 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00197 source Swiss-Prot : SWS_FT_FI3 18) 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 19) 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 20) chain B residue 268 type SITE sequence A description Important for dimerization => ECO:0000269|PubMed:23426375 source Swiss-Prot : SWS_FT_FI5

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