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 |