eF-site ID 1ldn-G PDB Code 1ldn Chain G click to enlarge Title STRUCTURE OF A TERNARY COMPLEX OF AN ALLOSTERIC LACTATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION Classification OXIDOREDUCTASE(CHOH(D)-NAD(A)) Compound L-LACTATE DEHYDROGENASE Source Geobacillus stearothermophilus (Bacillus stearothermophilus) (LDH_BACST) Sequence G:  MKNNGGARVVVIGAGFVGASYVFALMNQGIADEIVLIDAN ESKAIGDAMDFNHGKVFAPKPVDIWHGDYDDCRDADLVVI CAGANQKPGETRLDLVDKNIAIFRSIVESVMASGFQGLFL VATNPVDILTYATWKFSGLPHERVIGSGTILDTARFRFLL GEYFSVAPQNVHAYIIGEHGDTELPVWSQAYIGVMPIRKL VESKGEEAQKDLERIFVNVRDAAYQIIEKKGATYYGIAMG LARVTRAILHNENAILTVSAYLDGLYGERDVYIGVPAVIN RNGIREVIEIELNDDEKNRFHHSAATLKSVLARAFT Description Functional site 1) chain G residue 193 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN source Swiss-Prot : SWS_FT_FI1 2) chain G residue 30 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB source Swiss-Prot : SWS_FT_FI2 3) chain G residue 52 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB source Swiss-Prot : SWS_FT_FI2 4) chain G residue 136 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB source Swiss-Prot : SWS_FT_FI2 5) chain G residue 57 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00488 source Swiss-Prot : SWS_FT_FI3 6) chain G residue 83 type BINDING sequence Y description BINDING => ECO:0000255|HAMAP-Rule:MF_00488 source Swiss-Prot : SWS_FT_FI3 7) chain G residue 97 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00488 source Swiss-Prot : SWS_FT_FI3 8) chain G residue 100 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00488 source Swiss-Prot : SWS_FT_FI3 9) chain G residue 119 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00488 source Swiss-Prot : SWS_FT_FI3 10) chain G residue 138 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00488 source Swiss-Prot : SWS_FT_FI3 11) chain G residue 106 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN source Swiss-Prot : SWS_FT_FI4 12) chain G residue 166 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN source Swiss-Prot : SWS_FT_FI4 13) chain G residue 247 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN source Swiss-Prot : SWS_FT_FI4 14) chain G residue 161 type BINDING sequence S description BINDING => ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB source Swiss-Prot : SWS_FT_FI5 15) chain G residue 183 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB source Swiss-Prot : SWS_FT_FI5 16) chain G residue 171 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:2LDB source Swiss-Prot : SWS_FT_FI6 17) chain G residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488 source Swiss-Prot : SWS_FT_FI7

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