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 |