1O6Z
1.95 A resolution structure of (R207S,R292S) mutant of malate dehydrogenase from the halophilic archaeon Haloarcula marismortui (holo form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006089 | biological_process | lactate metabolic process |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006089 | biological_process | lactate metabolic process |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006089 | biological_process | lactate metabolic process |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A1001 |
| Chain | Residue |
| A | LYS205 |
| A | ASP306 |
| D | THR210 |
| D | ASP211 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A1005 |
| Chain | Residue |
| B | ASP73 |
| A | ARG166 |
| A | ARG252 |
| A | HIS256 |
| A | HOH2113 |
| B | TYR72 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B1003 |
| Chain | Residue |
| B | LYS205 |
| B | ASP306 |
| C | THR210 |
| C | ASP211 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B1006 |
| Chain | Residue |
| A | TYR72 |
| A | ASP73 |
| B | ARG166 |
| B | ARG252 |
| B | HIS256 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C1004 |
| Chain | Residue |
| B | THR210 |
| B | ASP211 |
| C | LYS205 |
| C | ASP306 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL C1007 |
| Chain | Residue |
| C | ARG166 |
| C | ARG252 |
| C | HIS256 |
| D | TYR72 |
| D | ASP73 |
| D | HOH2030 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D1002 |
| Chain | Residue |
| A | THR210 |
| A | ASP211 |
| D | LYS205 |
| D | ASP306 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL D1008 |
| Chain | Residue |
| C | TYR72 |
| C | ASP73 |
| D | ARG166 |
| D | ARG252 |
| D | HIS256 |
| D | HOH2129 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD A3001 |
| Chain | Residue |
| A | GLY30 |
| A | THR31 |
| A | VAL32 |
| A | ASP53 |
| A | LYS55 |
| A | THR97 |
| A | ALA98 |
| A | GLY99 |
| A | ILE119 |
| A | THR138 |
| A | ASN140 |
| A | VAL142 |
| A | PHE163 |
| A | GLY164 |
| A | LEU167 |
| A | HIS195 |
| A | HOH2004 |
| A | HOH2107 |
| A | HOH2156 |
| A | HOH2157 |
| A | HOH2159 |
| A | HOH2160 |
| site_id | BC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD B3002 |
| Chain | Residue |
| B | VAL27 |
| B | ALA29 |
| B | GLY30 |
| B | THR31 |
| B | VAL32 |
| B | ASP53 |
| B | ILE54 |
| B | LYS55 |
| B | TYR85 |
| B | THR97 |
| B | ALA98 |
| B | GLY99 |
| B | THR138 |
| B | ASN140 |
| B | VAL142 |
| B | PHE163 |
| B | LEU167 |
| B | HIS195 |
| B | HOH2165 |
| B | HOH2166 |
| B | HOH2168 |
| B | HOH2169 |
| B | HOH2170 |
| site_id | BC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD C3003 |
| Chain | Residue |
| C | HOH2044 |
| C | HOH2065 |
| C | HOH2123 |
| C | HOH2163 |
| C | HOH2164 |
| C | HOH2165 |
| C | GLY30 |
| C | THR31 |
| C | VAL32 |
| C | ASP53 |
| C | LYS55 |
| C | THR97 |
| C | ALA98 |
| C | GLY99 |
| C | ILE119 |
| C | THR138 |
| C | ASN140 |
| C | PHE163 |
| C | LEU167 |
| C | HIS195 |
| C | HOH2039 |
| site_id | BC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD D3004 |
| Chain | Residue |
| D | VAL27 |
| D | GLY28 |
| D | ALA29 |
| D | GLY30 |
| D | THR31 |
| D | VAL32 |
| D | ASP53 |
| D | LYS55 |
| D | TYR85 |
| D | THR97 |
| D | ALA98 |
| D | GLY99 |
| D | ILE119 |
| D | THR138 |
| D | ASN140 |
| D | VAL142 |
| D | LEU167 |
| D | HIS195 |
| D | HOH2178 |
| D | HOH2179 |
| D | HOH2180 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12581646","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS195 | |
| A | ASP168 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS195 | |
| B | ASP168 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS195 | |
| C | ASP168 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | HIS195 | |
| D | ASP168 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS195 | |
| A | ARG171 | |
| A | ASP168 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS195 | |
| B | ARG171 | |
| B | ASP168 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS195 | |
| C | ARG171 | |
| C | ASP168 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | HIS195 | |
| D | ARG171 | |
| D | ASP168 |
