2IV2
Reinterpretation of reduced form of formate dehydrogenase H from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| X | 0003954 | molecular_function | NADH dehydrogenase activity |
| X | 0005515 | molecular_function | protein binding |
| X | 0005829 | cellular_component | cytosol |
| X | 0006007 | biological_process | glucose catabolic process |
| X | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| X | 0009061 | biological_process | anaerobic respiration |
| X | 0009326 | cellular_component | formate dehydrogenase complex |
| X | 0015942 | biological_process | formate metabolic process |
| X | 0015944 | biological_process | formate oxidation |
| X | 0016020 | cellular_component | membrane |
| X | 0016491 | molecular_function | oxidoreductase activity |
| X | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
| X | 0019628 | biological_process | urate catabolic process |
| X | 0019645 | biological_process | anaerobic electron transport chain |
| X | 0043546 | molecular_function | molybdopterin cofactor binding |
| X | 0045271 | cellular_component | respiratory chain complex I |
| X | 0045333 | biological_process | cellular respiration |
| X | 0046872 | molecular_function | metal ion binding |
| X | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| X | 1990204 | cellular_component | oxidoreductase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 X 800 |
| Chain | Residue |
| X | CYS8 |
| X | PRO182 |
| X | ILE183 |
| X | TYR10 |
| X | CYS11 |
| X | SER13 |
| X | CYS15 |
| X | LEU41 |
| X | CYS42 |
| X | LYS44 |
| X | GLY45 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE 2MD X 801 |
| Chain | Residue |
| X | ARG110 |
| X | GLY111 |
| X | THR112 |
| X | CYS136 |
| X | GLN335 |
| X | GLY402 |
| X | GLU403 |
| X | ASP404 |
| X | THR408 |
| X | ALA410 |
| X | GLN428 |
| X | ASP429 |
| X | ILE430 |
| X | THR433 |
| X | SER445 |
| X | THR446 |
| X | HIS451 |
| X | ASP478 |
| X | CYS588 |
| X | SER590 |
| X | TYR678 |
| X | MGD802 |
| X | MO803 |
| X | UNX804 |
| X | HOH2155 |
| X | HOH2266 |
| X | HOH2267 |
| site_id | AC3 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE MGD X 802 |
| Chain | Residue |
| X | LYS44 |
| X | PHE173 |
| X | GLY174 |
| X | TYR175 |
| X | ASN176 |
| X | ASP179 |
| X | SER180 |
| X | CYS201 |
| X | ASP202 |
| X | PRO203 |
| X | ARG204 |
| X | ILE206 |
| X | GLY221 |
| X | ASN223 |
| X | GLY296 |
| X | MET297 |
| X | PHE302 |
| X | GLY334 |
| X | THR579 |
| X | VAL580 |
| X | ARG581 |
| X | GLU582 |
| X | VAL583 |
| X | HIS585 |
| X | TYR586 |
| X | SER587 |
| X | TYR651 |
| X | LYS679 |
| X | 2MD801 |
| X | MO803 |
| X | UNX804 |
| X | HOH2082 |
| X | HOH2084 |
| X | HOH2125 |
| X | HOH2259 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MO X 803 |
| Chain | Residue |
| X | 2MD801 |
| X | MGD802 |
| X | UNX804 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UNX X 804 |
| Chain | Residue |
| X | ALA137 |
| X | GLY334 |
| X | 2MD801 |
| X | MGD802 |
| X | MO803 |
Functional Information from PROSITE/UniProt
| site_id | PS00490 |
| Number of Residues | 18 |
| Details | MOLYBDOPTERIN_PROK_2 Prokaryotic molybdopterin oxidoreductases signature 2. TkTAsaADVILPsTSwgE |
| Chain | Residue | Details |
| X | THR433-GLU450 |
| site_id | PS00551 |
| Number of Residues | 18 |
| Details | MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. TvCpy.CASgCkInLvvd.N |
| Chain | Residue | Details |
| X | THR6-ASN23 |
| site_id | PS00932 |
| Number of Residues | 28 |
| Details | MOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AkrlGIeDeAlVwVhSrkGkiitrAqVS |
| Chain | Residue | Details |
| X | ALA615-SER642 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Electron donor/acceptor |
| Chain | Residue | Details |
| X | LYS44 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor |
| Chain | Residue | Details |
| X | SEC140 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01004, ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855 |
| Chain | Residue | Details |
| X | CYS8 | |
| X | TYR10 | |
| X | CYS11 | |
| X | CYS15 | |
| X | CYS42 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 11 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855 |
| Chain | Residue | Details |
| X | LYS44 | |
| X | TYR678 | |
| X | LYS679 | |
| X | MET297 | |
| X | GLN301 | |
| X | GLN335 | |
| X | SER445 | |
| X | ASP478 | |
| X | CYS588 | |
| X | TYR654 | |
| X | GLN655 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| X | ARG110 | |
| X | CYS661 | |
| X | SEC140 | |
| X | PHE173 | |
| X | CYS201 | |
| X | GLY221 | |
| X | GLY402 | |
| X | GLN428 | |
| X | THR579 | |
| X | ARG581 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity |
| Chain | Residue | Details |
| X | HIS141 | |
| X | ARG333 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| X | ASN132 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 562 |
| Chain | Residue | Details |
| X | LYS44 | electrostatic stabiliser |
| X | SEC140 | electrophile, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
| X | HIS141 | electrostatic stabiliser, proton acceptor |
| X | ARG333 | electrostatic stabiliser, hydrogen bond donor |
