2YIC
Crystal structure of the SucA domain of Mycobacterium smegmatis alpha- ketoglutarate decarboxylase (triclinic form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| C | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| C | 0030976 | molecular_function | thiamine pyrophosphate binding |
| D | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| D | 0030976 | molecular_function | thiamine pyrophosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TPP A 2001 |
| Chain | Residue |
| A | ARG540 |
| A | ILE680 |
| A | GLY681 |
| A | HIS747 |
| A | MG2002 |
| A | HOH3046 |
| A | HOH3048 |
| A | HOH3082 |
| A | HOH3083 |
| A | HOH3365 |
| B | GLN901 |
| A | SER604 |
| B | LEU950 |
| B | GLU952 |
| 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 | HOH3083 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 2003 |
| Chain | Residue |
| A | ASP1004 |
| A | HIS1055 |
| A | ASP1058 |
| A | ILE1060 |
| A | HOH3252 |
| A | HOH3253 |
| site_id | AC4 |
| Number of Residues | 23 |
| 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 | HOH3050 |
| B | HOH3083 |
| B | HOH3084 |
| B | HOH3104 |
| B | HOH3275 |
| 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 | HOH3084 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 2003 |
| Chain | Residue |
| B | ASP1004 |
| B | HIS1055 |
| B | ASP1058 |
| B | ILE1060 |
| B | HOH3198 |
| B | HOH3199 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE TPP C 2001 |
| Chain | Residue |
| C | ARG540 |
| C | SER604 |
| C | HIS605 |
| C | LEU606 |
| C | GLY644 |
| C | ASP645 |
| C | ALA646 |
| C | ALA647 |
| C | ASN678 |
| C | ILE680 |
| C | GLY681 |
| C | HIS747 |
| C | MG2002 |
| C | HOH3072 |
| C | HOH3073 |
| C | HOH3100 |
| C | HOH3338 |
| D | GLN901 |
| D | LEU950 |
| D | GLU952 |
| D | GLN976 |
| D | PHE980 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 2002 |
| Chain | Residue |
| C | ASP645 |
| C | ASN678 |
| C | ILE680 |
| C | TPP2001 |
| C | HOH3073 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 2003 |
| Chain | Residue |
| C | HOH3236 |
| C | HOH3237 |
| C | ASP1004 |
| C | HIS1055 |
| C | ASP1058 |
| C | ILE1060 |
| site_id | BC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE TPP D 2001 |
| Chain | Residue |
| C | GLN901 |
| C | LEU950 |
| C | GLU952 |
| C | GLN976 |
| C | PHE980 |
| D | ARG540 |
| D | SER604 |
| D | HIS605 |
| D | LEU606 |
| D | GLY644 |
| D | ASP645 |
| D | ALA646 |
| D | ALA647 |
| D | ASN678 |
| D | ILE680 |
| D | GLY681 |
| D | HIS747 |
| D | MG2002 |
| D | HOH3066 |
| D | HOH3067 |
| D | HOH3084 |
| D | HOH3243 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 2002 |
| Chain | Residue |
| D | ASP645 |
| D | ASN678 |
| D | ILE680 |
| D | TPP2001 |
| D | HOH3067 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 2003 |
| Chain | Residue |
| D | ASP1004 |
| D | HIS1055 |
| D | ASP1058 |
| D | ILE1060 |
| D | HOH3174 |
| D | HOH3175 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 60 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21867916, ECO:0007744|PDB:2XTA |
| Chain | Residue | Details |
| C | LEU606 | |
| C | ASP645 | |
| C | ALA646 | |
| C | ALA647 | |
| C | ASN678 | |
| C | ILE680 | |
| C | THR1038 | |
| C | ARG1054 | |
| C | LYS1089 | |
| C | SER1092 | |
| C | GLN1142 | |
| C | ARG1149 | |
| C | ARG1150 | |
| D | ARG540 | |
| D | SER604 | |
| D | LEU606 | |
| D | ASP645 | |
| D | ALA646 | |
| D | ALA647 | |
| D | ASN678 | |
| D | ILE680 | |
| D | THR1038 | |
| D | ARG1054 | |
| D | LYS1089 | |
| D | SER1092 | |
| D | GLN1142 | |
| D | ARG1149 | |
| D | ARG1150 | |
| A | ARG540 | |
| A | SER604 | |
| A | LEU606 | |
| A | ALA646 | |
| A | ALA647 | |
| A | ASN678 | |
| A | ILE680 | |
| A | THR1038 | |
| A | ARG1054 | |
| A | LYS1089 | |
| A | SER1092 | |
| A | GLN1142 | |
| A | ARG1149 | |
| A | ARG1150 | |
| B | ARG540 | |
| B | SER604 | |
| B | LEU606 | |
| B | ASP645 | |
| B | ALA646 | |
| B | ALA647 | |
| B | ASN678 | |
| B | ILE680 | |
| B | THR1038 | |
| B | ARG1054 | |
| B | LYS1089 | |
| B | SER1092 | |
| B | GLN1142 | |
| B | ARG1149 | |
| B | ARG1150 | |
| C | ARG540 | |
| C | SER604 | |
| A | ASP645 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:21867916, ECO:0007744|PDB:2Y0P |
| Chain | Residue | Details |
| A | HIS579 | |
| A | HIS1020 | |
| B | HIS579 | |
| B | HIS1020 | |
| C | HIS579 | |
| C | HIS1020 | |
| D | HIS579 | |
| D | HIS1020 |
