3ZHS
Crystal structure of the SucA domain of Mycobacterium smegmatis KGD, first post-decarboxylation intermediate from alpha-ketoglutarate
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 | 26 |
| Details | BINDING SITE FOR RESIDUE TD6 A 2001 |
| Chain | Residue |
| A | ARG540 |
| A | ILE680 |
| A | GLY681 |
| A | PHE682 |
| A | HIS747 |
| A | ASN748 |
| A | MG2002 |
| A | HOH3026 |
| A | HOH3042 |
| A | HOH3073 |
| A | HOH3074 |
| A | SER604 |
| A | HOH3316 |
| B | GLN901 |
| B | LEU950 |
| B | GLU952 |
| B | GLN976 |
| B | PHE980 |
| B | HIS1020 |
| 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 | TD62001 |
| A | HOH3074 |
| 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 | HOH3226 |
| A | HOH3227 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE TD6 B 2001 |
| Chain | Residue |
| A | GLN901 |
| A | LEU950 |
| A | GLU952 |
| A | GLN976 |
| A | PHE980 |
| A | HIS1020 |
| B | ARG505 |
| B | ARG540 |
| B | SER604 |
| B | HIS605 |
| B | LEU606 |
| B | GLY644 |
| B | ASP645 |
| B | ALA646 |
| B | ALA647 |
| B | ASN678 |
| B | ILE680 |
| B | GLY681 |
| B | PHE682 |
| B | HIS747 |
| B | ASN748 |
| B | MG2002 |
| B | HOH3037 |
| B | HOH3038 |
| B | HOH3039 |
| B | HOH3069 |
| B | HOH3070 |
| B | HOH3241 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 2002 |
| Chain | Residue |
| B | ASP645 |
| B | ASN678 |
| B | ILE680 |
| B | TD62001 |
| B | HOH3070 |
| 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 | HOH3174 |
| B | HOH3175 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE TD6 C 2001 |
| Chain | Residue |
| D | LEU950 |
| D | GLU952 |
| D | GLN976 |
| D | PHE980 |
| D | HIS1020 |
| C | ARG505 |
| C | ARG540 |
| C | SER604 |
| C | HIS605 |
| C | LEU606 |
| C | GLY644 |
| C | ASP645 |
| C | ALA646 |
| C | ALA647 |
| C | ASN678 |
| C | ILE680 |
| C | GLY681 |
| C | PHE682 |
| C | HIS747 |
| C | ASN748 |
| C | MG2002 |
| C | HOH3022 |
| C | HOH3034 |
| C | HOH3036 |
| C | HOH3063 |
| C | HOH3064 |
| C | HOH3272 |
| D | GLN901 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 2002 |
| Chain | Residue |
| C | ASP645 |
| C | ASN678 |
| C | ILE680 |
| C | TD62001 |
| C | HOH3064 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 2003 |
| Chain | Residue |
| C | ASP1004 |
| C | HIS1055 |
| C | ASP1058 |
| C | ILE1060 |
| C | HOH3203 |
| C | HOH3204 |
| site_id | BC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE TD6 D 2001 |
| Chain | Residue |
| C | GLN901 |
| C | LEU950 |
| C | GLU952 |
| C | GLN976 |
| C | PHE980 |
| C | HIS1020 |
| D | ARG540 |
| D | SER604 |
| D | HIS605 |
| D | LEU606 |
| D | GLY644 |
| D | ASP645 |
| D | ALA646 |
| D | ALA647 |
| D | ASN678 |
| D | ILE680 |
| D | GLY681 |
| D | PHE682 |
| D | HIS747 |
| D | ASN748 |
| D | MG2002 |
| D | HOH3033 |
| D | HOH3034 |
| D | HOH3060 |
| D | HOH3061 |
| D | HOH3211 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 2002 |
| Chain | Residue |
| D | ASP645 |
| D | ASN678 |
| D | ILE680 |
| D | TD62001 |
| D | HOH3061 |
| 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 | HOH3163 |
| D | HOH3164 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 60 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21867916","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XTA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21867916","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2Y0P","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
