6R2B
Crystal structure of the SucA domain of Mycobacterium smegmatis KGD after soaking with succinylphosphonate
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 | 32 |
| Details | binding site for residue QSP A 2001 |
| Chain | Residue |
| A | PHE506 |
| A | ASP645 |
| A | ALA646 |
| A | ALA647 |
| A | GLN651 |
| A | ASN678 |
| A | ILE680 |
| A | GLY681 |
| A | HIS747 |
| A | MG2002 |
| A | HOH2110 |
| A | HIS539 |
| A | HOH2137 |
| A | HOH2176 |
| A | HOH2200 |
| A | HOH2242 |
| A | HOH2279 |
| A | HOH2353 |
| B | GLN901 |
| B | LEU950 |
| B | GLU952 |
| B | GLN976 |
| A | ARG540 |
| B | PHE977 |
| B | PHE980 |
| B | HIS1020 |
| A | TYR578 |
| A | HIS579 |
| A | SER604 |
| A | HIS605 |
| A | LEU606 |
| A | GLY644 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 2002 |
| Chain | Residue |
| A | ASP645 |
| A | ASN678 |
| A | ILE680 |
| A | QSP2001 |
| A | HOH2279 |
| 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 | HOH2115 |
| A | HOH2394 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | binding site for residue QSP B 2001 |
| Chain | Residue |
| A | GLN901 |
| A | LEU950 |
| A | GLU952 |
| A | GLN976 |
| A | PHE977 |
| A | PHE980 |
| A | HIS1020 |
| B | PHE506 |
| B | HIS539 |
| B | ARG540 |
| B | TYR578 |
| B | HIS579 |
| B | SER604 |
| B | HIS605 |
| B | LEU606 |
| B | GLY644 |
| B | ASP645 |
| B | ALA646 |
| B | ALA647 |
| B | GLN651 |
| B | ASN678 |
| B | ILE680 |
| B | GLY681 |
| B | HIS747 |
| B | MG2002 |
| B | HOH2115 |
| B | HOH2142 |
| B | HOH2156 |
| B | HOH2208 |
| B | HOH2280 |
| B | HOH2304 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 2002 |
| Chain | Residue |
| B | ASP645 |
| B | ASN678 |
| B | ILE680 |
| B | QSP2001 |
| B | HOH2142 |
| 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 | HOH2201 |
| B | HOH2312 |
| site_id | AC7 |
| Number of Residues | 29 |
| Details | binding site for residue QSP C 2001 |
| Chain | Residue |
| C | HIS747 |
| C | MG2002 |
| C | HOH2112 |
| C | HOH2196 |
| C | HOH2200 |
| C | HOH2244 |
| C | HOH2308 |
| C | HOH2327 |
| D | GLN901 |
| D | LEU950 |
| D | GLU952 |
| D | GLN976 |
| D | PHE977 |
| D | PHE980 |
| D | HIS1020 |
| C | HIS539 |
| C | ARG540 |
| C | TYR578 |
| C | HIS579 |
| C | SER604 |
| C | HIS605 |
| C | LEU606 |
| C | GLY644 |
| C | ASP645 |
| C | ALA646 |
| C | ALA647 |
| C | ASN678 |
| C | ILE680 |
| C | GLY681 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 2002 |
| Chain | Residue |
| C | ASP645 |
| C | ASN678 |
| C | ILE680 |
| C | QSP2001 |
| C | HOH2244 |
| 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 | HOH2242 |
| C | HOH2403 |
| site_id | AD1 |
| Number of Residues | 32 |
| Details | binding site for residue QSP D 2001 |
| Chain | Residue |
| C | GLN901 |
| C | LEU950 |
| C | GLU952 |
| C | GLN976 |
| C | PHE977 |
| C | PHE980 |
| C | HIS1020 |
| D | PHE506 |
| D | HIS539 |
| D | ARG540 |
| D | TYR578 |
| D | HIS579 |
| D | SER604 |
| D | HIS605 |
| D | LEU606 |
| D | GLY644 |
| D | ASP645 |
| D | ALA646 |
| D | ALA647 |
| D | GLN651 |
| D | ASN678 |
| D | ILE680 |
| D | GLY681 |
| D | HIS747 |
| D | MG2002 |
| D | HOH2117 |
| D | HOH2129 |
| D | HOH2155 |
| D | HOH2217 |
| D | HOH2224 |
| D | HOH2238 |
| D | HOH2362 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 2002 |
| Chain | Residue |
| D | ASP645 |
| D | ASN678 |
| D | ILE680 |
| D | QSP2001 |
| D | HOH2217 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 2003 |
| Chain | Residue |
| D | ASP1004 |
| D | HIS1055 |
| D | ASP1058 |
| D | ILE1060 |
| D | HOH2125 |
| D | HOH2343 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 124 |
| Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| 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 |
