2GUG
NAD-dependent formate dehydrogenase from Pseudomonas sp.101 in complex with formate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| 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 | 0042183 | biological_process | formate catabolic process |
| A | 0051287 | molecular_function | NAD binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| 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 | 0042183 | biological_process | formate catabolic process |
| B | 0051287 | molecular_function | NAD binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0042183 | biological_process | formate catabolic process |
| C | 0051287 | molecular_function | NAD binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0042183 | biological_process | formate catabolic process |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 A 478 |
| Chain | Residue |
| A | SER184 |
| A | PEG480 |
| A | HOH526 |
| C | ASP13 |
| C | THR18 |
| C | TYR19 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 D 480 |
| Chain | Residue |
| D | GLU298 |
| D | TYR326 |
| D | HOH550 |
| B | THR18 |
| D | SER184 |
| D | HIS185 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT A 479 |
| Chain | Residue |
| A | PRO97 |
| A | PHE98 |
| A | GLY121 |
| A | ILE122 |
| A | ASN146 |
| A | PEG476 |
| A | HOH587 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT B 401 |
| Chain | Residue |
| B | PRO97 |
| B | PHE98 |
| B | ILE122 |
| B | ASN146 |
| B | HOH499 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT C 401 |
| Chain | Residue |
| C | PRO97 |
| C | PHE98 |
| C | GLY121 |
| C | ILE122 |
| C | ASN146 |
| C | HOH531 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEG A 476 |
| Chain | Residue |
| A | ILE122 |
| A | ASN146 |
| A | SER147 |
| A | VAL150 |
| A | ILE202 |
| A | THR282 |
| A | FMT479 |
| A | HOH554 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEG A 477 |
| Chain | Residue |
| A | PRO31 |
| A | TYR144 |
| A | ARG201 |
| A | ALA205 |
| A | ARG208 |
| A | ARG209 |
| C | GLU190 |
| C | ASP214 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 480 |
| Chain | Residue |
| A | GLU298 |
| A | TYR326 |
| A | PG4478 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PEG B 481 |
| Chain | Residue |
| B | LEU204 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG C 482 |
| Chain | Residue |
| C | ALA199 |
| C | GLY200 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG C 483 |
| Chain | Residue |
| C | GLU298 |
| C | TYR326 |
Functional Information from PROSITE/UniProt
| site_id | PS00065 |
| Number of Residues | 28 |
| Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGTVAaGRIGlavlrrlapfdvh.LHyTD |
| Chain | Residue | Details |
| A | VAL194-ASP221 |
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. MYpvCDVVtLNcPlhpeTehMiN |
| Chain | Residue | Details |
| A | MET244-ASN266 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. FKrGaYIVNtARGkLCD |
| Chain | Residue | Details |
| A | PHE273-ASP289 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|DOI:10.1134/S1063774506040146 |
| Chain | Residue | Details |
| A | GLY123 | |
| A | SER147 | |
| B | GLY123 | |
| B | SER147 | |
| C | GLY123 | |
| C | SER147 | |
| D | GLY123 | |
| D | SER147 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:8114093 |
| Chain | Residue | Details |
| A | ILE148 | |
| B | ILE202 | |
| B | ARG222 | |
| B | LEU257 | |
| B | ALA283 | |
| B | VAL309 | |
| B | ILE333 | |
| B | TYR381 | |
| C | ILE148 | |
| C | ILE202 | |
| C | ARG222 | |
| A | ILE202 | |
| C | LEU257 | |
| C | ALA283 | |
| C | VAL309 | |
| C | ILE333 | |
| C | TYR381 | |
| D | ILE148 | |
| D | ILE202 | |
| D | ARG222 | |
| D | LEU257 | |
| D | ALA283 | |
| A | ARG222 | |
| D | VAL309 | |
| D | ILE333 | |
| D | TYR381 | |
| A | LEU257 | |
| A | ALA283 | |
| A | VAL309 | |
| A | ILE333 | |
| A | TYR381 | |
| B | ILE148 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000305|PubMed:8114093 |
| Chain | Residue | Details |
| A | GLY285 | |
| A | ILE333 | |
| B | GLY285 | |
| B | ILE333 | |
| C | GLY285 | |
| C | ILE333 | |
| D | GLY285 | |
| D | ILE333 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 2nac |
| Chain | Residue | Details |
| A | GLN313 | |
| A | HIS332 | |
| A | ASN146 | |
| A | ARG284 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 2nac |
| Chain | Residue | Details |
| B | GLN313 | |
| B | HIS332 | |
| B | ASN146 | |
| B | ARG284 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 2nac |
| Chain | Residue | Details |
| C | GLN313 | |
| C | HIS332 | |
| C | ASN146 | |
| C | ARG284 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 2nac |
| Chain | Residue | Details |
| D | GLN313 | |
| D | HIS332 | |
| D | ASN146 | |
| D | ARG284 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 902 |
| Chain | Residue | Details |
| A | SER147 | electrostatic stabiliser |
| A | GLY285 | electrostatic stabiliser |
| A | PRO314 | modifies pKa |
| A | ILE333 | enhance reactivity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 902 |
| Chain | Residue | Details |
| B | SER147 | electrostatic stabiliser |
| B | GLY285 | electrostatic stabiliser |
| B | PRO314 | modifies pKa |
| B | ILE333 | enhance reactivity |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 902 |
| Chain | Residue | Details |
| C | SER147 | electrostatic stabiliser |
| C | GLY285 | electrostatic stabiliser |
| C | PRO314 | modifies pKa |
| C | ILE333 | enhance reactivity |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 902 |
| Chain | Residue | Details |
| D | SER147 | electrostatic stabiliser |
| D | GLY285 | electrostatic stabiliser |
| D | PRO314 | modifies pKa |
| D | ILE333 | enhance reactivity |
