1MLD
REFINED STRUCTURE OF MITOCHONDRIAL MALATE DEHYDROGENASE FROM PORCINE HEART AND THE CONSENSUS STRUCTURE FOR DICARBOXYLIC ACID OXIDOREDUCTASES
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006108 | biological_process | malate metabolic process |
| A | 0009060 | biological_process | aerobic respiration |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016615 | molecular_function | malate dehydrogenase 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 |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0051087 | molecular_function | protein-folding chaperone binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006108 | biological_process | malate metabolic process |
| B | 0009060 | biological_process | aerobic respiration |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016615 | molecular_function | malate dehydrogenase 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 |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0006108 | biological_process | malate metabolic process |
| C | 0009060 | biological_process | aerobic respiration |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016615 | molecular_function | malate dehydrogenase 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 |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0051087 | molecular_function | protein-folding chaperone binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0006108 | biological_process | malate metabolic process |
| D | 0009060 | biological_process | aerobic respiration |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016615 | molecular_function | malate dehydrogenase 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 |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0051087 | molecular_function | protein-folding chaperone binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CIT A 375 |
| Chain | Residue |
| A | ILE12 |
| A | HOH384 |
| A | HOH393 |
| A | HOH406 |
| A | HOH409 |
| A | ARG80 |
| A | ARG86 |
| A | ASN118 |
| A | ARG152 |
| A | HIS176 |
| A | GLY210 |
| A | ALA223 |
| A | HOH382 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CIT B 375 |
| Chain | Residue |
| B | ILE12 |
| B | ARG80 |
| B | ARG86 |
| B | ASN118 |
| B | LEU148 |
| B | ARG152 |
| B | HIS176 |
| B | GLY210 |
| B | ALA223 |
| B | MET227 |
| B | HOH388 |
| B | HOH390 |
| B | HOH398 |
| B | HOH411 |
| B | HOH414 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CIT C 375 |
| Chain | Residue |
| C | ILE12 |
| C | ARG80 |
| C | ARG86 |
| C | ASN118 |
| C | ARG152 |
| C | HIS176 |
| C | GLY210 |
| C | ALA223 |
| C | MET227 |
| C | HOH383 |
| C | HOH385 |
| C | HOH394 |
| C | HOH407 |
| C | HOH410 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CIT D 375 |
| Chain | Residue |
| D | ILE12 |
| D | ARG80 |
| D | ARG86 |
| D | ASN118 |
| D | ARG152 |
| D | HIS176 |
| D | GLY210 |
| D | HOH392 |
| D | HOH394 |
| D | HOH403 |
| D | HOH416 |
| D | HOH419 |
Functional Information from PROSITE/UniProt
| site_id | PS00068 |
| Number of Residues | 13 |
| Details | MDH Malate dehydrogenase active site signature. VTTLDivRAnafV |
| Chain | Residue | Details |
| A | VAL145-VAL157 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD |
| Chain | Residue | Details |
| A | ALA177 | |
| B | ALA177 | |
| C | ALA177 | |
| D | ALA177 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P40926 |
| Chain | Residue | Details |
| A | ALA8 | |
| B | ALA228 | |
| C | ALA8 | |
| C | ILE34 | |
| C | ALA94 | |
| C | SER117 | |
| C | ALA228 | |
| D | ALA8 | |
| D | ILE34 | |
| D | ALA94 | |
| D | SER117 | |
| A | ILE34 | |
| D | ALA228 | |
| A | ALA94 | |
| A | SER117 | |
| A | ALA228 | |
| B | ALA8 | |
| B | ILE34 | |
| B | ALA94 | |
| B | SER117 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD |
| Chain | Residue | Details |
| A | LYS81 | |
| C | ASP87 | |
| C | PRO119 | |
| C | ALA153 | |
| D | LYS81 | |
| D | ASP87 | |
| D | PRO119 | |
| D | ALA153 | |
| A | ASP87 | |
| A | PRO119 | |
| A | ALA153 | |
| B | LYS81 | |
| B | ASP87 | |
| B | PRO119 | |
| B | ALA153 | |
| C | LYS81 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 36 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 |
| Chain | Residue | Details |
| A | GLY55 | |
| B | GLY55 | |
| B | GLY68 | |
| B | GLY162 | |
| B | VAL192 | |
| B | LYS273 | |
| B | ILE284 | |
| B | MET291 | |
| B | ALA301 | |
| B | ASN312 | |
| C | GLY55 | |
| A | GLY68 | |
| C | GLY68 | |
| C | GLY162 | |
| C | VAL192 | |
| C | LYS273 | |
| C | ILE284 | |
| C | MET291 | |
| C | ALA301 | |
| C | ASN312 | |
| D | GLY55 | |
| D | GLY68 | |
| A | GLY162 | |
| D | GLY162 | |
| D | VAL192 | |
| D | LYS273 | |
| D | ILE284 | |
| D | MET291 | |
| D | ALA301 | |
| D | ASN312 | |
| A | VAL192 | |
| A | LYS273 | |
| A | ILE284 | |
| A | MET291 | |
| A | ALA301 | |
| A | ASN312 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P40926 |
| Chain | Residue | Details |
| A | ILE142 | |
| B | ILE142 | |
| C | ILE142 | |
| D | ILE142 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P08249 |
| Chain | Residue | Details |
| A | THR180 | |
| A | GLU246 | |
| B | THR180 | |
| B | GLU246 | |
| C | THR180 | |
| C | GLU246 | |
| D | THR180 | |
| D | GLU246 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 |
| Chain | Residue | Details |
| A | ALA216 | |
| D | ALA216 | |
| D | ASN278 | |
| D | LYS305 | |
| A | ASN278 | |
| A | LYS305 | |
| B | ALA216 | |
| B | ASN278 | |
| B | LYS305 | |
| C | ALA216 | |
| C | ASN278 | |
| C | LYS305 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P40926 |
| Chain | Residue | Details |
| A | ALA223 | |
| A | ILE303 | |
| B | ALA223 | |
| B | ILE303 | |
| C | ALA223 | |
| C | ILE303 | |
| D | ALA223 | |
| D | ILE303 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-malonyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 |
| Chain | Residue | Details |
| A | GLY306 | |
| B | GLY306 | |
| C | GLY306 | |
| D | GLY306 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P04636 |
| Chain | Residue | Details |
| A | GLY10 | |
| B | GLY10 | |
| C | GLY10 | |
| D | GLY10 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | ASP149 | |
| A | HIS176 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | ASP149 | |
| B | HIS176 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | ASP149 | |
| C | HIS176 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | ASP149 | |
| D | HIS176 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | ARG152 | |
| A | ASP149 | |
| A | HIS176 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | ARG152 | |
| B | ASP149 | |
| B | HIS176 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | ARG152 | |
| C | ASP149 | |
| C | HIS176 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| D | ARG152 | |
| D | ASP149 | |
| D | HIS176 |
