2DFV
Hyperthermophilic threonine dehydrogenase from Pyrococcus horikoshii
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0006566 | biological_process | threonine metabolic process |
A | 0006567 | biological_process | threonine catabolic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008743 | molecular_function | L-threonine 3-dehydrogenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016597 | molecular_function | amino acid binding |
A | 0019518 | biological_process | L-threonine catabolic process to glycine |
A | 0030554 | molecular_function | adenyl nucleotide binding |
A | 0043168 | molecular_function | anion binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0051262 | biological_process | protein tetramerization |
A | 0051289 | biological_process | protein homotetramerization |
A | 0070401 | molecular_function | NADP+ binding |
A | 0070403 | molecular_function | NAD+ binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006566 | biological_process | threonine metabolic process |
B | 0006567 | biological_process | threonine catabolic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008743 | molecular_function | L-threonine 3-dehydrogenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016597 | molecular_function | amino acid binding |
B | 0019518 | biological_process | L-threonine catabolic process to glycine |
B | 0030554 | molecular_function | adenyl nucleotide binding |
B | 0043168 | molecular_function | anion binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0051262 | biological_process | protein tetramerization |
B | 0051289 | biological_process | protein homotetramerization |
B | 0070401 | molecular_function | NADP+ binding |
B | 0070403 | molecular_function | NAD+ binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006566 | biological_process | threonine metabolic process |
C | 0006567 | biological_process | threonine catabolic process |
C | 0008270 | molecular_function | zinc ion binding |
C | 0008743 | molecular_function | L-threonine 3-dehydrogenase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016597 | molecular_function | amino acid binding |
C | 0019518 | biological_process | L-threonine catabolic process to glycine |
C | 0030554 | molecular_function | adenyl nucleotide binding |
C | 0043168 | molecular_function | anion binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0051262 | biological_process | protein tetramerization |
C | 0051289 | biological_process | protein homotetramerization |
C | 0070401 | molecular_function | NADP+ binding |
C | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1001 |
Chain | Residue |
A | CYS97 |
A | CYS100 |
A | CYS103 |
A | CYS111 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 1002 |
Chain | Residue |
B | CYS97 |
B | CYS100 |
B | CYS103 |
B | CYS111 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 1003 |
Chain | Residue |
C | CYS100 |
C | CYS103 |
C | CYS111 |
C | CYS97 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 2001 |
Chain | Residue |
A | HIS94 |
A | ASN156 |
A | GLY293 |
A | ARG294 |
A | NAD1401 |
A | HOH2186 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 2002 |
Chain | Residue |
B | HIS94 |
B | ASN156 |
B | GLY293 |
B | ARG294 |
B | NAD2401 |
B | HOH2403 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 2003 |
Chain | Residue |
C | HIS94 |
C | ASN156 |
C | GLY293 |
C | ARG294 |
C | NAD3401 |
C | HOH3403 |
site_id | AC7 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NAD A 1401 |
Chain | Residue |
A | CYS42 |
A | ASN156 |
A | GLY175 |
A | GLY177 |
A | PRO178 |
A | LEU179 |
A | SER198 |
A | GLU199 |
A | PRO200 |
A | ARG204 |
A | PHE243 |
A | SER244 |
A | ALA246 |
A | ALA249 |
A | LEU266 |
A | GLY267 |
A | LEU268 |
A | ILE282 |
A | ILE291 |
A | THR292 |
A | SO42001 |
A | HOH2010 |
A | HOH2028 |
A | HOH2029 |
A | HOH2038 |
A | HOH2053 |
A | HOH2137 |
A | HOH2152 |
A | HOH2153 |
A | HOH2154 |
A | HOH2166 |
site_id | AC8 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD B 2401 |
Chain | Residue |
B | CYS42 |
B | ASN156 |
B | GLY175 |
B | GLY177 |
B | PRO178 |
B | LEU179 |
B | SER198 |
B | GLU199 |
B | PRO200 |
B | ARG204 |
B | PHE243 |
B | SER244 |
B | ALA246 |
B | LEU266 |
B | GLY267 |
B | LEU268 |
B | ILE291 |
B | THR292 |
B | SO42002 |
B | HOH2413 |
B | HOH2423 |
B | HOH2426 |
B | HOH2443 |
B | HOH2493 |
B | HOH2521 |
B | HOH2537 |
B | HOH2560 |
C | ILE282 |
site_id | AC9 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD C 3401 |
Chain | Residue |
C | ARG204 |
C | PHE243 |
C | SER244 |
C | ALA246 |
C | LEU266 |
C | GLY267 |
C | LEU268 |
C | ILE291 |
C | THR292 |
C | SO42003 |
C | HOH3407 |
C | HOH3420 |
C | HOH3451 |
C | HOH3484 |
C | HOH3495 |
C | HOH3513 |
C | HOH3536 |
B | ILE282 |
C | CYS42 |
C | ASN156 |
C | GLY175 |
C | GLY177 |
C | PRO178 |
C | LEU179 |
C | SER198 |
C | GLU199 |
C | PRO200 |
Functional Information from PROSITE/UniProt
site_id | PS00059 |
Number of Residues | 15 |
Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEvAGEvveiGpgV |
Chain | Residue | Details |
A | GLY66-VAL80 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Charge relay system => ECO:0000305|PubMed:18390572 |
Chain | Residue | Details |
A | THR44 | |
A | HIS47 | |
B | THR44 | |
B | HIS47 | |
C | THR44 | |
C | HIS47 |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000269|Ref.5, ECO:0000305|PubMed:17188300, ECO:0000305|PubMed:18390572, ECO:0007744|PDB:2D8A |
Chain | Residue | Details |
A | CYS42 | |
A | HIS67 | |
A | GLU68 | |
B | CYS42 | |
B | HIS67 | |
B | GLU68 | |
C | CYS42 | |
C | HIS67 | |
C | GLU68 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000269|PubMed:17188300, ECO:0007744|PDB:2DFV |
Chain | Residue | Details |
A | CYS97 | |
C | CYS100 | |
C | CYS103 | |
C | CYS111 | |
A | CYS100 | |
A | CYS103 | |
A | CYS111 | |
B | CYS97 | |
B | CYS100 | |
B | CYS103 | |
B | CYS111 | |
C | CYS97 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17188300, ECO:0000269|Ref.5 |
Chain | Residue | Details |
A | LEU179 | |
B | LEU179 | |
C | LEU179 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17188300, ECO:0000269|Ref.5, ECO:0007744|PDB:2D8A, ECO:0007744|PDB:2DFV |
Chain | Residue | Details |
A | GLU199 | |
A | ARG204 | |
B | GLU199 | |
B | ARG204 | |
C | GLU199 | |
C | ARG204 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|Ref.5, ECO:0007744|PDB:2D8A |
Chain | Residue | Details |
A | LEU266 | |
A | ILE291 | |
B | LEU266 | |
B | ILE291 | |
C | LEU266 | |
C | ILE291 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | SITE: Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atom => ECO:0000305|PubMed:18390572 |
Chain | Residue | Details |
A | GLU152 | |
B | GLU152 | |
C | GLU152 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
A | THR44 | |
A | GLY43 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
B | THR44 | |
B | GLY43 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
C | THR44 | |
C | GLY43 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
A | THR44 | |
A | HIS47 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
B | THR44 | |
B | HIS47 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
C | THR44 | |
C | HIS47 |