2XT6
Crystal structure of Mycobacterium smegmatis alpha-ketoglutarate decarboxylase homodimer (orthorhombic form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004149 | molecular_function | dihydrolipoyllysine-residue succinyltransferase activity |
| A | 0004591 | molecular_function | oxoglutarate dehydrogenase (succinyl-transferring) activity |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0008683 | molecular_function | 2-oxoglutarate decarboxylase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050439 | molecular_function | 2-hydroxy-3-oxoadipate synthase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004149 | molecular_function | dihydrolipoyllysine-residue succinyltransferase activity |
| B | 0004591 | molecular_function | oxoglutarate dehydrogenase (succinyl-transferring) activity |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0008683 | molecular_function | 2-oxoglutarate decarboxylase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050439 | molecular_function | 2-hydroxy-3-oxoadipate synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TPP A 2001 |
| Chain | Residue |
| A | ARG540 |
| A | ILE680 |
| A | GLY681 |
| A | HIS747 |
| A | MG2002 |
| A | HOH3017 |
| A | HOH3054 |
| A | HOH3055 |
| B | GLN901 |
| B | LEU950 |
| B | GLU952 |
| A | SER604 |
| B | GLN976 |
| B | PHE980 |
| A | HIS605 |
| A | LEU606 |
| A | GLY644 |
| A | ASP645 |
| A | ALA646 |
| A | ALA647 |
| A | ASN678 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 2002 |
| Chain | Residue |
| A | ASP645 |
| A | ASN678 |
| A | ILE680 |
| A | TPP2001 |
| A | HOH3017 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 2003 |
| Chain | Residue |
| A | ASP1004 |
| A | HIS1055 |
| A | ASP1058 |
| A | ILE1060 |
| A | HOH3043 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE TPP B 2001 |
| Chain | Residue |
| A | GLN901 |
| A | LEU950 |
| A | GLU952 |
| A | GLN976 |
| A | PHE980 |
| B | ARG540 |
| B | SER604 |
| B | HIS605 |
| B | LEU606 |
| B | GLY644 |
| B | ASP645 |
| B | ALA646 |
| B | ALA647 |
| B | ASN678 |
| B | ILE680 |
| B | GLY681 |
| B | HIS747 |
| B | MG2002 |
| B | HOH3021 |
| B | HOH3060 |
| B | HOH3062 |
| B | HOH3063 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 2002 |
| Chain | Residue |
| B | ASP645 |
| B | ASN678 |
| B | ILE680 |
| B | TPP2001 |
| B | HOH3062 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 2003 |
| Chain | Residue |
| B | ASP1004 |
| B | HIS1055 |
| B | ASP1058 |
| B | ILE1060 |
| B | HOH3051 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor; for succinyltransferase activity => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS314 | |
| B | HIS314 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21867916, ECO:0007744|PDB:2XTA |
| Chain | Residue | Details |
| A | ARG540 | |
| A | ARG1054 | |
| A | LYS1089 | |
| A | SER1092 | |
| A | GLN1142 | |
| A | ARG1149 | |
| A | ARG1150 | |
| B | ARG540 | |
| B | SER604 | |
| B | LEU606 | |
| B | ASP645 | |
| A | SER604 | |
| B | ALA646 | |
| B | ALA647 | |
| B | ASN678 | |
| B | ILE680 | |
| B | THR1038 | |
| B | ARG1054 | |
| B | LYS1089 | |
| B | SER1092 | |
| B | GLN1142 | |
| B | ARG1149 | |
| A | LEU606 | |
| B | ARG1150 | |
| A | ASP645 | |
| A | ALA646 | |
| A | ALA647 | |
| A | ASN678 | |
| A | ILE680 | |
| A | THR1038 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:21867916, ECO:0007744|PDB:2Y0P |
| Chain | Residue | Details |
| A | HIS579 | |
| A | HIS1020 | |
| B | HIS579 | |
| B | HIS1020 |
