1B0V
I40N MUTANT OF AZOTOBACTER VINELANDII FDI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0003677 | molecular_function | DNA binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 A 107 |
| Chain | Residue |
| A | PHE2 |
| A | CYS45 |
| A | CYS20 |
| A | VAL22 |
| A | CYS24 |
| A | PHE25 |
| A | CYS39 |
| A | ASN40 |
| A | CYS42 |
| A | ALA43 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE F3S A 108 |
| Chain | Residue |
| A | CYS8 |
| A | LYS12 |
| A | TYR13 |
| A | THR14 |
| A | ASP15 |
| A | CYS16 |
| A | LEU32 |
| A | CYS49 |
| A | PRO50 |
| A | ILE54 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 B 307 |
| Chain | Residue |
| B | PHE202 |
| B | CYS220 |
| B | VAL222 |
| B | CYS224 |
| B | PHE225 |
| B | CYS239 |
| B | ASN240 |
| B | CYS242 |
| B | ALA243 |
| B | CYS245 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F3S B 308 |
| Chain | Residue |
| B | CYS208 |
| B | LYS212 |
| B | TYR213 |
| B | THR214 |
| B | ASP215 |
| B | CYS216 |
| B | LEU232 |
| B | CYS249 |
| B | PRO250 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 C 507 |
| Chain | Residue |
| C | PHE402 |
| C | CYS420 |
| C | VAL422 |
| C | CYS424 |
| C | PHE425 |
| C | ILE434 |
| C | CYS439 |
| C | ASN440 |
| C | CYS442 |
| C | ALA443 |
| C | CYS445 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE F3S C 508 |
| Chain | Residue |
| C | CYS408 |
| C | TYR413 |
| C | THR414 |
| C | ASP415 |
| C | CYS416 |
| C | LEU432 |
| C | CYS449 |
| C | ILE454 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 D 707 |
| Chain | Residue |
| D | PHE602 |
| D | CYS620 |
| D | VAL622 |
| D | CYS624 |
| D | PHE625 |
| D | ILE634 |
| D | CYS639 |
| D | ASN640 |
| D | CYS642 |
| D | ALA643 |
| D | CYS645 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE F3S D 708 |
| Chain | Residue |
| D | CYS608 |
| D | TYR613 |
| D | THR614 |
| D | ASP615 |
| D | CYS616 |
| D | LEU632 |
| D | CYS649 |
| D | ILE654 |
Functional Information from PROSITE/UniProt
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CnDCAlCEpECP |
| Chain | Residue | Details |
| A | CYS39-PRO50 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:3422475 |
| Chain | Residue | Details |
| A | ILE9 | |
| B | PRO221 | |
| B | ASN240 | |
| B | ALA243 | |
| B | GLU246 | |
| B | PRO250 | |
| C | ILE409 | |
| C | VAL417 | |
| C | PRO421 | |
| C | ASN440 | |
| C | ALA443 | |
| A | VAL17 | |
| C | GLU446 | |
| C | PRO450 | |
| D | ILE609 | |
| D | VAL617 | |
| D | PRO621 | |
| D | ASN640 | |
| D | ALA643 | |
| D | GLU646 | |
| D | PRO650 | |
| A | PRO21 | |
| A | ASN40 | |
| A | ALA43 | |
| A | GLU46 | |
| A | PRO50 | |
| B | ILE209 | |
| B | VAL217 |
