2CMD
THE CRYSTAL STRUCTURE OF E.COLI MALATE DEHYDROGENASE: A COMPLEX OF THE APOENZYME AND CITRATE AT 1.87 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006108 | biological_process | malate metabolic process |
| A | 0006113 | biological_process | fermentation |
| A | 0009061 | biological_process | anaerobic respiration |
| A | 0016020 | cellular_component | membrane |
| 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 | 0019898 | cellular_component | extrinsic component of membrane |
| A | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CIT A 313 |
| Chain | Residue |
| A | ARG153 |
| A | HIS177 |
| A | GLY210 |
| A | HOH335 |
| A | HOH353 |
| A | HOH354 |
| A | HOH369 |
| A | HOH404 |
| A | ILE12 |
| A | ARG81 |
| A | ARG87 |
| A | ASN119 |
| site_id | ACT |
| Number of Residues | 5 |
| Details |
| Chain | Residue |
| A | ARG81 |
| A | ARG87 |
| A | ASP150 |
| A | ARG153 |
| A | HIS177 |
Functional Information from PROSITE/UniProt
| site_id | PS00068 |
| Number of Residues | 13 |
| Details | MDH Malate dehydrogenase active site signature. VTTLDiiRSntfV |
| Chain | Residue | Details |
| A | VAL146-VAL158 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389141","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389141","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8331658","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1507230","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8331658","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS177 | |
| A | ASP150 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS177 | |
| A | ASP150 | |
| A | ARG153 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 527 |
| Chain | Residue | Details |
| A | ASP150 | modifies pKa |
| A | HIS177 | proton acceptor, proton donor |
