eF-site ID 1gqz-A PDB Code 1gqz Chain A click to enlarge Title Refinement of Haemophilus influenzae Diaminopimelate epimerase at 1.7A Classification ISOMERASE Compound DIAMINOPIMELATE EPIMERASE Source null (DAPF_HAEIN) Sequence A:  MQFSKMHGLGNDFVVVDGVTQNVFFTPETIRRLANRHCGI GFDQLLIVEAPYDPELDFHYRIFNADGSEVSQCGNGARCF ARFVTLKGLTNKKDISVSTQKGNMVLTVKDDNQIRVNMGE PIWEPAKIPFTANKFEKNYILRTDIQTVLCGAVSMGNPHC VVQVDDIQTANVEQLGPLLESHERFPERVNAGFMQIINKE HIKLRVYERGAGETQACGSGACAAVAVGIMQGLLNNNVQV DLPGGSLMIEWNGVGHPLYMTGEATHIYDGFITL Description Functional site 1) chain A residue 73 type catalytic sequence C description 334 source MCSA : MCSA1 2) chain A residue 159 type catalytic sequence H description 334 source MCSA : MCSA1 3) chain A residue 208 type catalytic sequence E description 334 source MCSA : MCSA1 4) chain A residue 217 type catalytic sequence C description 334 source MCSA : MCSA1 5) chain A residue 220 type catalytic sequence G description 334 source MCSA : MCSA1 6) chain A residue 268 type SITE sequence Y description Important for dimerization => ECO:0000250|UniProtKB:P0A6K1 source Swiss-Prot : SWS_FT_FI6 7) chain A residue 73 type ACT_SITE sequence C description Proton donor => ECO:0000305|PubMed:16723397, ECO:0000305|PubMed:9843410, ECO:0000305|DOI:10.1021/ja001193t, ECO:0007744|PDB:1BWZ, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ source Swiss-Prot : SWS_FT_FI1 8) chain A residue 217 type ACT_SITE sequence C description Proton acceptor => ECO:0000305|PubMed:16723397, ECO:0000305|PubMed:9843410, ECO:0000305|DOI:10.1021/ja001193t, ECO:0007744|PDB:1BWZ, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ source Swiss-Prot : SWS_FT_FI2 9) chain A residue 64 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ source Swiss-Prot : SWS_FT_FI3 10) chain A residue 190 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ source Swiss-Prot : SWS_FT_FI3 11) chain A residue 208 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ source Swiss-Prot : SWS_FT_FI3 12) chain A residue 218 type BINDING sequence G description BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ source Swiss-Prot : SWS_FT_FI3 13) chain A residue 74 type BINDING sequence G description BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ source Swiss-Prot : SWS_FT_FI3 14) chain A residue 157 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ source Swiss-Prot : SWS_FT_FI3 15) chain A residue 11 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ source Swiss-Prot : SWS_FT_FI3 16) chain A residue 44 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKJ source Swiss-Prot : SWS_FT_FI4 17) chain A residue 208 type SITE sequence E description Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000305|PubMed:9843410, ECO:0007744|PDB:1BWZ source Swiss-Prot : SWS_FT_FI5 18) chain A residue 159 type SITE sequence H description Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000305|PubMed:9843410, ECO:0007744|PDB:1BWZ source Swiss-Prot : SWS_FT_FI5 19) chain A residue 64-78 type prosite sequence NADGSEVSQCGNGAR description DAP_EPIMERASE Diaminopimelate epimerase signature. NaDGSevsqCGNGaR source prosite : PS01326

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