1H0H
Tungsten containing Formate Dehydrogenase from Desulfovibrio Gigas
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0043546 | molecular_function | molybdopterin cofactor binding |
| A | 0045333 | biological_process | cellular respiration |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047111 | molecular_function | formate dehydrogenase (cytochrome-c-553) activity |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| K | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| K | 0009055 | molecular_function | electron transfer activity |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0042597 | cellular_component | periplasmic space |
| K | 0043546 | molecular_function | molybdopterin cofactor binding |
| K | 0045333 | biological_process | cellular respiration |
| K | 0046872 | molecular_function | metal ion binding |
| K | 0047111 | molecular_function | formate dehydrogenase (cytochrome-c-553) activity |
| K | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| L | 0042597 | cellular_component | periplasmic space |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 1100 |
| Chain | Residue |
| A | THR358 |
| A | LYS360 |
| A | LYS363 |
| A | LEU393 |
| A | GLY394 |
| A | ASN395 |
| A | HOH2328 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA K 1100 |
| Chain | Residue |
| K | LYS363 |
| K | LEU393 |
| K | GLY394 |
| K | ASN395 |
| K | HOH2287 |
| K | THR358 |
| K | LYS360 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE W A 1000 |
| Chain | Residue |
| A | SEC158 |
| A | 2MD1001 |
| A | MGD1002 |
| A | UNX1003 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE W K 1000 |
| Chain | Residue |
| K | SEC158 |
| K | 2MD1001 |
| K | MGD1002 |
| K | UNX1003 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE 2MD A 1001 |
| Chain | Residue |
| A | ALA130 |
| A | GLN154 |
| A | ILE157 |
| A | SEC158 |
| A | MET371 |
| A | GLU409 |
| A | GLY516 |
| A | GLN517 |
| A | ASN518 |
| A | SER522 |
| A | VAL542 |
| A | ASN543 |
| A | ILE544 |
| A | CYS572 |
| A | ALA573 |
| A | LYS578 |
| A | ASP605 |
| A | THR854 |
| A | ARG856 |
| A | GLN862 |
| A | THR863 |
| A | LEU865 |
| A | MET866 |
| A | TRP936 |
| A | ASN951 |
| A | THR967 |
| A | W1000 |
| A | MGD1002 |
| A | UNX1003 |
| A | HOH2646 |
| A | HOH2692 |
| A | HOH2697 |
| site_id | AC6 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE MGD A 1002 |
| Chain | Residue |
| A | LYS56 |
| A | SEC158 |
| A | GLY192 |
| A | SER193 |
| A | ASN194 |
| A | GLU197 |
| A | ASN198 |
| A | VAL219 |
| A | ASP220 |
| A | PRO221 |
| A | ARG222 |
| A | SER238 |
| A | GLY239 |
| A | ASP241 |
| A | ALA370 |
| A | MET371 |
| A | TRP373 |
| A | GLY408 |
| A | TYR855 |
| A | ARG856 |
| A | VAL857 |
| A | THR858 |
| A | HIS860 |
| A | TRP861 |
| A | GLN862 |
| A | HIS937 |
| A | LYS968 |
| A | W1000 |
| A | 2MD1001 |
| A | UNX1003 |
| A | HOH2053 |
| A | HOH2317 |
| A | HOH2700 |
| A | HOH2701 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE UNX A 1003 |
| Chain | Residue |
| A | SEC158 |
| A | GLU409 |
| A | VAL412 |
| A | W1000 |
| A | 2MD1001 |
| A | MGD1002 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 A 1010 |
| Chain | Residue |
| A | CYS54 |
| A | GLY57 |
| A | PRO200 |
| A | ILE201 |
| A | CYS17 |
| A | TYR19 |
| A | CYS20 |
| A | CYS24 |
| A | LEU53 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EPE A 1200 |
| Chain | Residue |
| A | HOH2702 |
| A | HOH2703 |
| A | HOH2704 |
| B | PRO42 |
| B | ASP43 |
| B | ASP123 |
| B | ARG126 |
| B | TYR211 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B 1011 |
| Chain | Residue |
| B | CYS11 |
| B | THR12 |
| B | ALA13 |
| B | CYS14 |
| B | ARG15 |
| B | CYS17 |
| B | CYS156 |
| B | THR158 |
| B | MET161 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 B 1012 |
| Chain | Residue |
| B | PHE4 |
| B | CYS21 |
| B | HIS25 |
| B | GLN71 |
| B | CYS137 |
| B | ASP138 |
| B | MET139 |
| B | CYS140 |
| B | PRO150 |
| B | CYS152 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B 1013 |
| Chain | Residue |
| B | CYS72 |
| B | ARG73 |
| B | CYS75 |
| B | PRO79 |
| B | CYS80 |
| B | CYS120 |
| B | TYR122 |
| B | PRO125 |
| B | LYS136 |
| site_id | BC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE 2MD K 1001 |
| Chain | Residue |
| K | ALA130 |
| K | GLN154 |
| K | ILE157 |
| K | SEC158 |
| K | MET371 |
| K | GLU409 |
| K | GLY516 |
| K | GLN517 |
| K | ASN518 |
| K | SER522 |
| K | VAL542 |
| K | ASN543 |
| K | ILE544 |
| K | CYS572 |
| K | ALA573 |
| K | LYS578 |
| K | ASP605 |
| K | THR854 |
| K | ARG856 |
| K | GLN862 |
| K | THR863 |
| K | LEU865 |
| K | MET866 |
| K | TRP936 |
| K | ASN951 |
| K | THR967 |
| K | W1000 |
| K | MGD1002 |
| K | UNX1003 |
| K | HOH2561 |
| K | HOH2611 |
| K | HOH2618 |
| site_id | BC5 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE MGD K 1002 |
| Chain | Residue |
| K | LYS56 |
| K | SEC158 |
| K | GLY192 |
| K | SER193 |
| K | ASN194 |
| K | GLU197 |
| K | ASN198 |
| K | VAL219 |
| K | ASP220 |
| K | PRO221 |
| K | ARG222 |
| K | SER238 |
| K | GLY239 |
| K | ASP241 |
| K | ALA370 |
| K | MET371 |
| K | TRP373 |
| K | GLY408 |
| K | TYR855 |
| K | ARG856 |
| K | VAL857 |
| K | THR858 |
| K | HIS860 |
| K | TRP861 |
| K | GLN862 |
| K | HIS937 |
| K | LYS968 |
| K | W1000 |
| K | 2MD1001 |
| K | UNX1003 |
| K | HOH2162 |
| K | HOH2276 |
| K | HOH2612 |
| K | HOH2619 |
| K | HOH2620 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE UNX K 1003 |
| Chain | Residue |
| K | SEC158 |
| K | GLU409 |
| K | VAL412 |
| K | W1000 |
| K | 2MD1001 |
| K | MGD1002 |
| site_id | BC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 K 1010 |
| Chain | Residue |
| K | CYS17 |
| K | TYR19 |
| K | CYS20 |
| K | GLY23 |
| K | CYS24 |
| K | LEU53 |
| K | CYS54 |
| K | LYS56 |
| K | GLY57 |
| K | PRO200 |
| K | ILE201 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EPE K 1200 |
| Chain | Residue |
| K | HOH2623 |
| L | PRO42 |
| L | ASP43 |
| L | ASP123 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 L 1011 |
| Chain | Residue |
| L | CYS11 |
| L | THR12 |
| L | ALA13 |
| L | CYS14 |
| L | ARG15 |
| L | CYS17 |
| L | CYS156 |
| L | THR158 |
| L | MET161 |
| site_id | CC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 L 1012 |
| Chain | Residue |
| L | PHE4 |
| L | CYS21 |
| L | HIS25 |
| L | LYS50 |
| L | GLN71 |
| L | CYS137 |
| L | ASP138 |
| L | MET139 |
| L | CYS140 |
| L | PRO150 |
| L | CYS152 |
| site_id | CC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 L 1013 |
| Chain | Residue |
| L | CYS72 |
| L | ARG73 |
| L | CYS75 |
| L | PRO79 |
| L | CYS80 |
| L | CYS120 |
| L | TYR122 |
| L | PRO125 |
| L | LYS136 |
Functional Information from PROSITE/UniProt
| site_id | PS00551 |
| Number of Residues | 19 |
| Details | MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. SvCcy.CSVgCgLiVhtdkK |
| Chain | Residue | Details |
| A | SER15-LYS33 |
| site_id | PS00932 |
| Number of Residues | 28 |
| Details | MOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AtlrGIkNgDkViLeSvrGklwakAiIT |
| Chain | Residue | Details |
| A | ALA889-THR916 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11372198 |
| Chain | Residue | Details |
| B | CYS11 | |
| B | CYS140 | |
| B | CYS152 | |
| B | CYS156 | |
| L | CYS11 | |
| L | CYS14 | |
| L | CYS17 | |
| L | CYS21 | |
| L | CYS72 | |
| L | CYS75 | |
| L | CYS80 | |
| B | CYS14 | |
| L | CYS120 | |
| L | CYS137 | |
| L | CYS140 | |
| L | CYS152 | |
| L | CYS156 | |
| B | CYS17 | |
| B | CYS21 | |
| B | CYS72 | |
| B | CYS75 | |
| B | CYS80 | |
| B | CYS120 | |
| B | CYS137 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12220497 |
| Chain | Residue | Details |
| A | SEC158 | |
| K | SEC158 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1H0H |
| Chain | Residue | Details |
| A | THR358 | |
| K | ASN395 | |
| A | LYS360 | |
| A | LYS363 | |
| A | LEU393 | |
| A | ASN395 | |
| K | THR358 | |
| K | LYS360 | |
| K | LYS363 | |
| K | LEU393 |
