2G8Y
The structure of a putative malate/lactate dehydrogenase from E. coli.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0047029 | molecular_function | (R)-4-hydroxyphenyllactate dehydrogenase (NADP+) activity |
| A | 0047995 | molecular_function | (2R)-hydroxyphenylpyruvate reductase [NAD(P)H] activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0047029 | molecular_function | (R)-4-hydroxyphenyllactate dehydrogenase (NADP+) activity |
| B | 0047995 | molecular_function | (2R)-hydroxyphenylpyruvate reductase [NAD(P)H] activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1003 |
| Chain | Residue |
| A | HIS48 |
| A | THR162 |
| A | ALA187 |
| A | PHE188 |
| A | GLY189 |
| A | NAD1001 |
| A | SO41007 |
| A | EDO1018 |
| A | EDO1019 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1004 |
| Chain | Residue |
| A | ARG6 |
| A | ARG323 |
| A | HOH1334 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1005 |
| Chain | Residue |
| B | HIS45 |
| B | ASP46 |
| B | SER47 |
| B | HIS48 |
| B | SO41008 |
| B | HOH1041 |
| B | HOH1119 |
| B | HOH1127 |
| B | HOH1444 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1006 |
| Chain | Residue |
| B | ARG58 |
| B | ARG192 |
| B | ALA337 |
| B | HOH1179 |
| B | HOH1224 |
| B | HOH1325 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1007 |
| Chain | Residue |
| A | HIS45 |
| A | ASP46 |
| A | SER47 |
| A | HIS48 |
| A | NAD1001 |
| A | SO41003 |
| A | HOH1295 |
| A | HOH1451 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1008 |
| Chain | Residue |
| B | HIS48 |
| B | PHE188 |
| B | GLY189 |
| B | NAD1002 |
| B | SO41005 |
| B | EDO1013 |
| B | HOH1378 |
| B | HOH1380 |
| B | HOH1422 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1009 |
| Chain | Residue |
| B | ARG320 |
| B | GLN324 |
| B | HOH1301 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1010 |
| Chain | Residue |
| B | ARG21 |
| site_id | AC9 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAD A 1001 |
| Chain | Residue |
| A | HIS45 |
| A | HIS48 |
| A | HIS120 |
| A | GLY122 |
| A | ARG123 |
| A | ILE124 |
| A | VAL144 |
| A | THR162 |
| A | PRO164 |
| A | LEU178 |
| A | LEU179 |
| A | ASP180 |
| A | TYR181 |
| A | ALA182 |
| A | ALA187 |
| A | ASN270 |
| A | GLY313 |
| A | GLU316 |
| A | SO41003 |
| A | SO41007 |
| A | EDO1019 |
| A | HOH1023 |
| A | HOH1025 |
| A | HOH1071 |
| A | HOH1112 |
| A | HOH1138 |
| A | HOH1256 |
| A | HOH1295 |
| A | HOH1312 |
| A | HOH1347 |
| B | PHE153 |
| B | HIS234 |
| B | LYS235 |
| B | TYR237 |
| B | HOH1135 |
| B | HOH1243 |
| site_id | BC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD B 1002 |
| Chain | Residue |
| B | LEU179 |
| B | ASP180 |
| B | TYR181 |
| B | ALA182 |
| B | ALA187 |
| B | ASN270 |
| B | GLY313 |
| B | GLU316 |
| B | SO41008 |
| B | EDO1013 |
| B | HOH1127 |
| B | HOH1134 |
| B | HOH1201 |
| B | HOH1241 |
| B | HOH1262 |
| B | HOH1306 |
| B | HOH1378 |
| A | PHE153 |
| A | HIS234 |
| A | LYS235 |
| A | TYR237 |
| A | HOH1130 |
| B | HIS45 |
| B | HIS48 |
| B | HIS120 |
| B | GLY122 |
| B | ARG123 |
| B | ILE124 |
| B | VAL144 |
| B | THR162 |
| B | PRO164 |
| B | LEU178 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 1011 |
| Chain | Residue |
| A | GLN221 |
| A | GLU350 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1012 |
| Chain | Residue |
| B | HIS106 |
| B | ALA134 |
| B | GLY135 |
| B | ASN278 |
| B | GLU280 |
| B | HOH1034 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 1013 |
| Chain | Residue |
| B | HIS48 |
| B | HIS120 |
| B | MSE149 |
| B | THR162 |
| B | NAD1002 |
| B | SO41008 |
| B | HOH1374 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1014 |
| Chain | Residue |
| B | ARG6 |
| B | GLU322 |
| B | ARG323 |
| B | HOH1331 |
| B | HOH1332 |
| B | HOH1432 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1015 |
| Chain | Residue |
| A | GLN290 |
| B | LYS254 |
| B | HIS257 |
| B | GLU259 |
| B | THR260 |
| B | HOH1443 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1016 |
| Chain | Residue |
| A | GLN10 |
| A | HOH1305 |
| A | HOH1396 |
| A | HOH1397 |
| A | HOH1400 |
| A | HOH1433 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1017 |
| Chain | Residue |
| A | HIS154 |
| A | HOH1370 |
| A | HOH1449 |
| B | LYS307 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1018 |
| Chain | Residue |
| A | ARG192 |
| A | SO41003 |
| A | HOH1257 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1019 |
| Chain | Residue |
| A | HIS48 |
| A | HIS120 |
| A | MSE149 |
| A | THR162 |
| A | NAD1001 |
| A | SO41003 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 1020 |
| Chain | Residue |
| B | SER47 |
| B | GLY189 |
| B | ARG192 |
| B | HOH1320 |
| site_id | CC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1021 |
| Chain | Residue |
| A | TRP60 |
| A | TRP60 |
| A | SER61 |
| A | SER61 |
| A | HOH1043 |
| A | HOH1342 |
| A | HOH1355 |
| A | HOH1358 |
| A | HOH1358 |
| A | HOH1398 |
| A | HOH1398 |
| A | HOH1418 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"The structure of a putative malate/lactate dehydrogenase from E. coli.","authors":["Cuff M.E.","Skarina T.","Edwards A.","Savchenko A.","Cymborowski M.","Minor W.","Joachimiak A."]}},{"source":"PDB","id":"2G8Y","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1s20 |
| Chain | Residue | Details |
| A | HIS48 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1s20 |
| Chain | Residue | Details |
| B | HIS48 |
