2G37
Structure of Thermus thermophilus L-proline dehydrogenase
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 | 23 |
Details | BINDING SITE FOR RESIDUE FAD A 2001 |
Chain | Residue |
A | ASP133 |
A | TYR190 |
A | LYS201 |
A | ALA225 |
A | THR226 |
A | HIS227 |
A | ASP228 |
A | PRO229 |
A | GLN252 |
A | LEU254 |
A | VAL257 |
A | MET134 |
A | ARG258 |
A | TYR275 |
A | ARG293 |
A | HOH2003 |
A | VAL161 |
A | GLN163 |
A | ARG184 |
A | VAL186 |
A | LYS187 |
A | GLY188 |
A | ALA189 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE FAD B 2002 |
Chain | Residue |
B | ASP133 |
B | MET134 |
B | VAL161 |
B | GLN163 |
B | ARG184 |
B | VAL186 |
B | LYS187 |
B | GLY188 |
B | ALA189 |
B | TYR190 |
B | ALA225 |
B | THR226 |
B | HIS227 |
B | ASP228 |
B | PRO229 |
B | LEU254 |
B | VAL257 |
B | TYR275 |
B | HOH2003 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD B 371 |
Chain | Residue |
B | PHE129 |
B | ASN182 |
B | TYR221 |
B | GLU250 |
B | ARG273 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD B 372 |
Chain | Residue |
A | GLY30 |
A | ARG33 |
A | ARG34 |
A | HOH2080 |
B | ARG151 |
B | PRO178 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MPD A 373 |
Chain | Residue |
A | LYS94 |
A | PHE129 |
A | ARG131 |
A | ASN182 |
A | TYR221 |
A | GLU250 |
A | ARG273 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD A 374 |
Chain | Residue |
A | ARG151 |
A | PRO178 |
A | HOH2043 |
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 |