2EKG
Structure of Thermus thermophilus Proline Dehydrogenase inactivated by N-propargylglycine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004657 | molecular_function | proline dehydrogenase activity |
| A | 0006560 | biological_process | proline metabolic process |
| A | 0006562 | biological_process | L-proline catabolic process |
| A | 0010133 | biological_process | L-proline catabolic process to L-glutamate |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0071949 | molecular_function | FAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004657 | molecular_function | proline dehydrogenase activity |
| B | 0006560 | biological_process | proline metabolic process |
| B | 0006562 | biological_process | L-proline catabolic process |
| B | 0010133 | biological_process | L-proline catabolic process to L-glutamate |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE FAD A 2001 |
| Chain | Residue |
| A | ASP133 |
| A | ASP228 |
| A | PRO229 |
| A | GLN252 |
| A | TYR275 |
| A | HOH2023 |
| A | HOH2173 |
| A | MET134 |
| A | GLN163 |
| A | ARG184 |
| A | LYS187 |
| A | GLY188 |
| A | ALA189 |
| A | THR226 |
| A | HIS227 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE FAD B 2002 |
| Chain | Residue |
| B | ASP133 |
| B | MET134 |
| B | GLN163 |
| B | ARG184 |
| B | LYS187 |
| B | GLY188 |
| B | ALA189 |
| B | ALA225 |
| B | THR226 |
| B | HIS227 |
| B | ASP228 |
| B | PRO229 |
| B | GLN252 |
| B | TYR275 |
| B | HOH2089 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD B 1371 |
| Chain | Residue |
| B | PHE129 |
| B | ARG131 |
| B | ASN182 |
| B | TYR221 |
| B | GLU250 |
| B | ARG273 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD B 1372 |
| Chain | Residue |
| A | GLY30 |
| A | ARG33 |
| A | ARG34 |
| A | HOH2126 |
| B | ARG151 |
| B | TYR179 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD A 1373 |
| Chain | Residue |
| A | LYS94 |
| A | PHE129 |
| A | ARG131 |
| A | ASN182 |
| A | TYR221 |
| A | GLU250 |
| A | ARG273 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 1374 |
| Chain | Residue |
| A | ARG151 |
| A | HOH2151 |
| B | LYS194 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"18426222","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9RW55","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17344208","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18426222","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2EKG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G37","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17344208","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2G37","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Critical for catalytic activity","evidences":[{"source":"PubMed","id":"18426222","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
