1WZE
Structural basis for alteration of cofactor specificity of Malate dehydrogenase from Thermus flavus
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 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 activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE NAD A 1334 |
Chain | Residue |
A | GLY13 |
A | HIS186 |
A | SER240 |
A | ALA245 |
A | HOH1382 |
A | GLN14 |
A | ILE15 |
A | VAL86 |
A | VAL128 |
A | GLY129 |
A | ASN130 |
A | MET154 |
A | LEU157 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE NAD B 2334 |
Chain | Residue |
B | GLY13 |
B | GLN14 |
B | ILE15 |
B | VAL86 |
B | VAL128 |
B | GLY129 |
B | ASN130 |
B | MET154 |
B | HIS186 |
B | SER240 |
B | HOH2337 |
B | HOH2357 |
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 |