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 | proline catabolic process |
| A | 0010133 | biological_process | proline catabolic process to 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 | proline catabolic process |
| B | 0010133 | biological_process | proline catabolic process to 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 | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:18426222 |
| Chain | Residue | Details |
| A | ASP133 | |
| A | ARG184 | |
| B | ASP133 | |
| B | ARG184 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9RW55 |
| Chain | Residue | Details |
| A | LYX99 | |
| A | ARG288 | |
| B | LYX99 | |
| B | ARG288 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17344208, ECO:0000269|PubMed:18426222, ECO:0007744|PDB:2EKG, ECO:0007744|PDB:2G37 |
| Chain | Residue | Details |
| A | MET134 | |
| A | GLN163 | |
| A | LYS187 | |
| A | THR226 | |
| B | MET134 | |
| B | GLN163 | |
| B | LYS187 | |
| B | THR226 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17344208, ECO:0007744|PDB:2G37 |
| Chain | Residue | Details |
| A | LYS201 | |
| B | LYS201 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Critical for catalytic activity => ECO:0000305|PubMed:18426222 |
| Chain | Residue | Details |
| A | TYR275 | |
| B | TYR275 |
