2O4C
Crystal Structure of D-Erythronate-4-phosphate Dehydrogenase Complexed with NAD
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008615 | biological_process | pyridoxine biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0033711 | molecular_function | 4-phosphoerythronate dehydrogenase activity |
A | 0036001 | biological_process | 'de novo' pyridoxal 5'-phosphate biosynthetic process |
A | 0046983 | molecular_function | protein dimerization activity |
A | 0051287 | molecular_function | NAD binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008615 | biological_process | pyridoxine biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0033711 | molecular_function | 4-phosphoerythronate dehydrogenase activity |
B | 0036001 | biological_process | 'de novo' pyridoxal 5'-phosphate biosynthetic process |
B | 0046983 | molecular_function | protein dimerization activity |
B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 900 |
Chain | Residue |
A | ARG44 |
A | SER45 |
A | THR66 |
A | TYR258 |
A | ARG346 |
site_id | AC2 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD B 1001 |
Chain | Residue |
B | GLY125 |
B | GLN126 |
B | VAL127 |
B | CYS145 |
B | ASP146 |
B | PRO147 |
B | PRO148 |
B | HIS174 |
B | THR175 |
B | PRO176 |
B | HIS183 |
B | THR185 |
B | ALA206 |
B | SER207 |
B | ARG208 |
B | ASP232 |
B | HIS254 |
B | ALA256 |
B | GLY257 |
B | HOH2652 |
B | HOH2661 |
B | HOH2702 |
B | ASN91 |
B | VAL95 |
B | VAL122 |
B | GLY123 |
site_id | AC3 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD A 1002 |
Chain | Residue |
A | ASN91 |
A | VAL95 |
A | GLY123 |
A | GLY125 |
A | GLN126 |
A | VAL127 |
A | CYS145 |
A | ASP146 |
A | PRO147 |
A | PRO148 |
A | HIS174 |
A | THR175 |
A | PRO176 |
A | HIS183 |
A | THR185 |
A | ALA206 |
A | SER207 |
A | ARG208 |
A | ASP232 |
A | HIS254 |
A | ALA256 |
A | GLY257 |
A | HOH1003 |
A | HOH1004 |
A | HOH1008 |
A | HOH1038 |
A | HOH1060 |
A | HOH1084 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE TLA B 500 |
Chain | Residue |
B | ARG208 |
B | HIS254 |
B | TYR258 |
B | ARG346 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 2647 |
Chain | Residue |
B | LEU138 |
B | TRP140 |
B | ALA307 |
B | HOH2676 |
Functional Information from PROSITE/UniProt
site_id | PS00671 |
Number of Residues | 17 |
Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. LRpGtWLVNaSRGaVVD |
Chain | Residue | Details |
A | LEU197-ASP213 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01825, ECO:0000305|PubMed:17217963 |
Chain | Residue | Details |
A | ARG208 | |
A | GLU237 | |
B | ARG208 | |
B | GLU237 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01825, ECO:0000305|PubMed:17217963 |
Chain | Residue | Details |
A | HIS254 | |
B | HIS254 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01825, ECO:0000305|PubMed:17217963 |
Chain | Residue | Details |
A | SER45 | |
A | THR66 | |
A | TYR258 | |
B | SER45 | |
B | THR66 | |
B | TYR258 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01825, ECO:0000269|PubMed:17217963 |
Chain | Residue | Details |
A | GLN126 | |
B | ALA206 | |
B | ASP232 | |
B | GLY257 | |
A | ASP146 | |
A | THR175 | |
A | ALA206 | |
A | ASP232 | |
A | GLY257 | |
B | GLN126 | |
B | ASP146 | |
B | THR175 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1psd |
Chain | Residue | Details |
A | HIS254 | |
A | GLU237 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1psd |
Chain | Residue | Details |
B | HIS254 | |
B | GLU237 |