4PLT
Crystal structure of ancestral apicomplexan malate dehydrogenase with oxamate.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
A | 0006089 | biological_process | lactate metabolic process |
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 |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
B | 0006089 | biological_process | lactate metabolic process |
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 |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
C | 0006089 | biological_process | lactate metabolic process |
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 |
D | 0000166 | molecular_function | nucleotide binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
D | 0006089 | biological_process | lactate metabolic process |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 34 |
Details | binding site for residue NAI B 401 |
Chain | Residue |
B | GLY13 |
B | THR79 |
B | ALA80 |
B | GLY81 |
B | ILE82 |
B | PRO83 |
B | ASN102 |
B | ILE105 |
B | VAL125 |
B | ASN127 |
B | LEU129 |
B | ASN14 |
B | MET150 |
B | LEU154 |
B | HIS182 |
B | ALA237 |
B | PRO241 |
B | OXM402 |
B | HOH519 |
B | HOH522 |
B | HOH525 |
B | HOH549 |
B | ILE15 |
B | HOH564 |
B | HOH612 |
B | HOH619 |
B | HOH632 |
B | HOH733 |
B | PHE34 |
B | ASP35 |
B | ILE36 |
B | VAL37 |
B | MET40 |
B | TYR67 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue OXM B 402 |
Chain | Residue |
B | TRP93 |
B | ARG95 |
B | ASN127 |
B | ARG158 |
B | HIS182 |
B | GLY225 |
B | ALA237 |
B | NAI401 |
B | HOH550 |
B | HOH612 |
site_id | AC3 |
Number of Residues | 33 |
Details | binding site for residue NAI A 401 |
Chain | Residue |
A | GLY13 |
A | ASN14 |
A | ILE15 |
A | PHE34 |
A | ASP35 |
A | ILE36 |
A | VAL37 |
A | MET40 |
A | TYR67 |
A | THR79 |
A | ALA80 |
A | GLY81 |
A | ILE82 |
A | PRO83 |
A | ILE105 |
A | VAL125 |
A | THR126 |
A | ASN127 |
A | MET150 |
A | LEU154 |
A | HIS182 |
A | ALA237 |
A | OXM402 |
A | HOH522 |
A | HOH527 |
A | HOH537 |
A | HOH554 |
A | HOH561 |
A | HOH599 |
A | HOH625 |
A | HOH642 |
A | HOH661 |
A | HOH725 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue OXM A 402 |
Chain | Residue |
A | TRP93 |
A | ARG95 |
A | ASN127 |
A | ARG158 |
A | HIS182 |
A | ALA237 |
A | NAI401 |
A | HOH537 |
A | HOH544 |
site_id | AC5 |
Number of Residues | 35 |
Details | binding site for residue NAI C 401 |
Chain | Residue |
C | PRO83 |
C | ASN102 |
C | ILE105 |
C | VAL125 |
C | THR126 |
C | ASN127 |
C | LEU129 |
C | MET150 |
C | LEU154 |
C | HIS182 |
C | ALA237 |
C | PRO241 |
C | OXM402 |
C | HOH527 |
C | HOH545 |
C | HOH563 |
C | HOH572 |
C | HOH573 |
C | HOH583 |
C | HOH589 |
C | HOH604 |
C | HOH673 |
C | GLY13 |
C | ASN14 |
C | ILE15 |
C | PHE34 |
C | ASP35 |
C | ILE36 |
C | VAL37 |
C | MET40 |
C | TYR67 |
C | THR79 |
C | ALA80 |
C | GLY81 |
C | ILE82 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue OXM C 402 |
Chain | Residue |
C | TRP93 |
C | ARG95 |
C | ASN127 |
C | ARG158 |
C | HIS182 |
C | GLY225 |
C | NAI401 |
C | HOH544 |
C | HOH572 |
site_id | AC7 |
Number of Residues | 34 |
Details | binding site for residue NAI D 401 |
Chain | Residue |
D | GLY13 |
D | ASN14 |
D | ILE15 |
D | PHE34 |
D | ASP35 |
D | ILE36 |
D | VAL37 |
D | MET40 |
D | THR79 |
D | ALA80 |
D | GLY81 |
D | ILE82 |
D | PRO83 |
D | LEU98 |
D | ASN102 |
D | ILE105 |
D | VAL125 |
D | ASN127 |
D | MET150 |
D | LEU154 |
D | HIS182 |
D | ALA237 |
D | PRO241 |
D | OXM402 |
D | HOH520 |
D | HOH548 |
D | HOH549 |
D | HOH556 |
D | HOH566 |
D | HOH574 |
D | HOH609 |
D | HOH619 |
D | HOH629 |
D | HOH652 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue OXM D 402 |
Chain | Residue |
D | TRP93 |
D | ARG95 |
D | ASN127 |
D | ARG158 |
D | HIS182 |
D | NAI401 |
D | HOH524 |
D | HOH566 |