2X0R
R207S, R292S Mutant of Malate Dehydrogenase from the Halophilic Archeon Haloarcula marismortui (HoloForm)
Replaces: 1GT2Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006089 | biological_process | lactate metabolic process |
| A | 0006090 | biological_process | pyruvate metabolic process |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| 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 |
| A | 0030060 | molecular_function | L-malate dehydrogenase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0006090 | biological_process | pyruvate metabolic process |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| 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 |
| B | 0030060 | molecular_function | L-malate dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD A 607 |
| Chain | Residue |
| A | GLY28 |
| A | GLY99 |
| A | ILE123 |
| A | THR138 |
| A | SER139 |
| A | ASN140 |
| A | PHE163 |
| A | LEU167 |
| A | HIS195 |
| A | HOH2048 |
| A | GLY30 |
| A | THR31 |
| A | VAL32 |
| A | ASP53 |
| A | ILE54 |
| A | LYS55 |
| A | THR97 |
| A | ALA98 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1001 |
| Chain | Residue |
| A | LYS205 |
| A | ASP306 |
| B | ASP211 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 1004 |
| Chain | Residue |
| A | ARG43 |
| A | ARG252 |
| A | ALA255 |
| A | HIS256 |
| A | GLU259 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 1007 |
| Chain | Residue |
| A | ASP44 |
| A | ALA46 |
| A | ASP47 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD B 608 |
| Chain | Residue |
| B | VAL27 |
| B | ALA29 |
| B | GLY30 |
| B | THR31 |
| B | VAL32 |
| B | ASP53 |
| B | THR97 |
| B | ALA98 |
| B | GLY99 |
| B | ARG102 |
| B | THR138 |
| B | SER139 |
| B | ASN140 |
| B | VAL142 |
| B | PHE163 |
| B | HIS195 |
| B | HOH2001 |
| B | HOH2018 |
| B | HOH2019 |
| B | HOH2071 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1002 |
| Chain | Residue |
| A | THR210 |
| A | ASP211 |
| B | LYS205 |
| B | ASP306 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 1005 |
| Chain | Residue |
| B | ARG43 |
| B | ARG252 |
| B | ALA255 |
| B | HIS256 |
| B | GLU259 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA B 1006 |
| Chain | Residue |
| A | HOH2029 |
| B | LYS205 |
| B | SER207 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 1008 |
| Chain | Residue |
| B | ILE40 |
| B | ALA41 |
| B | ASP44 |
| B | ILE45 |
| B | ALA46 |
| B | THR76 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE NA B 1009 |
| Chain | Residue |
| B | GLN80 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 1010 |
| Chain | Residue |
| B | ASP143 |
| B | ASN146 |
| B | SER272 |
| B | ALA286 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P61889 |
| Chain | Residue | Details |
| A | HIS195 | |
| B | HIS195 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12581646 |
| Chain | Residue | Details |
| A | ASN116 | |
| A | THR138 | |
| B | GLY28 | |
| B | ASP53 | |
| B | ASN116 | |
| B | THR138 | |
| A | GLY28 | |
| A | ASP53 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P61889 |
| Chain | Residue | Details |
| B | ARG102 | |
| B | ARG109 | |
| B | ASN140 | |
| B | ARG171 | |
| A | ARG102 | |
| A | ARG109 | |
| A | ASN140 | |
| A | ARG171 |
