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 (NAD+) 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 (NAD+) 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 | GLY28 | |
A | ASP53 | |
A | ASN116 | |
A | THR138 | |
B | GLY28 | |
B | ASP53 | |
B | ASN116 | |
B | THR138 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P61889 |
Chain | Residue | Details |
A | ARG102 | |
A | ARG109 | |
A | ASN140 | |
A | ARG171 | |
B | ARG102 | |
B | ARG109 | |
B | ASN140 | |
B | ARG171 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
A | HIS195 | |
A | ASP168 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
B | HIS195 | |
B | ASP168 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
A | HIS195 | |
A | ARG171 | |
A | ASP168 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
B | HIS195 | |
B | ARG171 | |
B | ASP168 |