2CVQ
Crystal structure of NAD(H)-dependent malate dehydrogenase complexed with NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006107 | biological_process | oxaloacetate metabolic process |
| A | 0006108 | biological_process | malate metabolic process |
| A | 0006734 | biological_process | NADH metabolic process |
| 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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006107 | biological_process | oxaloacetate metabolic process |
| B | 0006108 | biological_process | malate metabolic process |
| B | 0006734 | biological_process | NADH metabolic process |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NDP A 334 |
| Chain | Residue |
| A | GLY10 |
| A | VAL128 |
| A | GLY129 |
| A | ASN130 |
| A | LEU157 |
| A | SER240 |
| A | SER241 |
| A | ALA245 |
| A | TRS4617 |
| A | TRS4619 |
| B | LYS220 |
| A | GLY13 |
| A | GLN14 |
| A | ILE15 |
| A | GLU41 |
| A | ILE42 |
| A | ALA45 |
| A | VAL86 |
| A | ALA88 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NDP B 1334 |
| Chain | Residue |
| A | LYS220 |
| B | GLY13 |
| B | GLN14 |
| B | ILE15 |
| B | GLU41 |
| B | ILE42 |
| B | ALA45 |
| B | VAL86 |
| B | ALA88 |
| B | VAL128 |
| B | GLY129 |
| B | ASN130 |
| B | LEU157 |
| B | SER240 |
| B | SER241 |
| B | ALA245 |
| B | TRS4621 |
| B | TRS4623 |
| B | HOH4650 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TRS A 4617 |
| Chain | Residue |
| A | GLY230 |
| A | NDP334 |
| A | TRS4619 |
| A | HOH4623 |
| A | HOH4628 |
| A | HOH4662 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TRS A 4619 |
| Chain | Residue |
| A | ASN130 |
| A | LEU157 |
| A | ASP158 |
| A | ARG161 |
| A | HIS186 |
| A | NDP334 |
| A | TRS4617 |
| A | HOH4628 |
| A | HOH4645 |
| A | HOH4673 |
| A | HOH4731 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TRS B 4621 |
| Chain | Residue |
| B | ASN130 |
| B | GLY230 |
| B | SER240 |
| B | NDP1334 |
| B | TRS4623 |
| B | HOH4631 |
| B | HOH4636 |
| B | HOH4783 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TRS B 4623 |
| Chain | Residue |
| B | ASN130 |
| B | LEU157 |
| B | ASP158 |
| B | HIS186 |
| B | NDP1334 |
| B | TRS4621 |
| B | HOH4629 |
| B | HOH4631 |
| B | HOH4669 |
| B | HOH4715 |
Functional Information from PROSITE/UniProt
| site_id | PS00068 |
| Number of Residues | 13 |
| Details | MDH Malate dehydrogenase active site signature. MTRLDhnRAkaqL |
| Chain | Residue | Details |
| A | MET154-LEU166 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01517 |
| Chain | Residue | Details |
| A | HIS186 | |
| B | HIS186 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:16009341, ECO:0000269|PubMed:8471603 |
| Chain | Residue | Details |
| A | GLY10 | |
| A | VAL128 | |
| B | GLY10 | |
| B | VAL128 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01517 |
| Chain | Residue | Details |
| A | ARG91 | |
| B | ARG161 | |
| A | ARG97 | |
| A | ASN104 | |
| A | ASN130 | |
| A | ARG161 | |
| B | ARG91 | |
| B | ARG97 | |
| B | ASN104 | |
| B | ASN130 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:16009341 |
| Chain | Residue | Details |
| A | GLN111 | |
| B | GLN111 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | ASN185 | |
| A | ASP158 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | ASN185 | |
| B | ASP158 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS186 | |
| A | ARG161 | |
| A | ASP158 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS186 | |
| B | ARG161 | |
| B | ASP158 |
