1BDM
THE STRUCTURE AT 1.8 ANGSTROMS RESOLUTION OF A SINGLE SITE MUTANT (T189I) OF MALATE DEHYDROGENASE FROM THERMUS FLAVUS WITH INCREASED ENZYMATIC ACTIVITY
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 | 23 |
Details | BINDING SITE FOR RESIDUE NAX A 334 |
Chain | Residue |
A | GLY10 |
A | GLN111 |
A | VAL128 |
A | GLY129 |
A | ASN130 |
A | MET154 |
A | HIS186 |
A | ALA245 |
A | HOH767 |
A | HOH795 |
A | HOH904 |
A | GLY13 |
A | HOH907 |
A | HOH913 |
A | HOH916 |
A | HOH950 |
A | GLN14 |
A | ILE15 |
A | GLU41 |
A | ILE42 |
A | VAL86 |
A | GLY87 |
A | ALA88 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAX B 334 |
Chain | Residue |
B | GLY10 |
B | GLY13 |
B | GLN14 |
B | ILE15 |
B | GLU41 |
B | ILE42 |
B | VAL86 |
B | GLY87 |
B | ALA88 |
B | ILE107 |
B | GLN111 |
B | VAL128 |
B | GLY129 |
B | ASN130 |
B | MET154 |
B | HIS186 |
B | ALA245 |
B | HOH765 |
B | HOH784 |
B | HOH866 |
B | HOH922 |
B | HOH933 |
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 |