4Q5I
Crystal structure of a T151A mutant of the E. coli FeoB G-domain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005525 | molecular_function | GTP binding |
| A | 0006826 | biological_process | iron ion transport |
| A | 0015093 | molecular_function | ferrous iron transmembrane transporter activity |
| A | 0016020 | cellular_component | membrane |
| B | 0005525 | molecular_function | GTP binding |
| B | 0006826 | biological_process | iron ion transport |
| B | 0015093 | molecular_function | ferrous iron transmembrane transporter activity |
| B | 0016020 | cellular_component | membrane |
| C | 0005525 | molecular_function | GTP binding |
| C | 0006826 | biological_process | iron ion transport |
| C | 0015093 | molecular_function | ferrous iron transmembrane transporter activity |
| C | 0016020 | cellular_component | membrane |
| D | 0005525 | molecular_function | GTP binding |
| D | 0006826 | biological_process | iron ion transport |
| D | 0015093 | molecular_function | ferrous iron transmembrane transporter activity |
| D | 0016020 | cellular_component | membrane |
| E | 0005525 | molecular_function | GTP binding |
| E | 0006826 | biological_process | iron ion transport |
| E | 0015093 | molecular_function | ferrous iron transmembrane transporter activity |
| E | 0016020 | cellular_component | membrane |
| F | 0005525 | molecular_function | GTP binding |
| F | 0006826 | biological_process | iron ion transport |
| F | 0015093 | molecular_function | ferrous iron transmembrane transporter activity |
| F | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 301 |
| Chain | Residue |
| D | GLY10 |
| D | ASN11 |
| D | THR60 |
| D | ASN91 |
| D | VAL92 |
| D | ASN101 |
| D | LEU104 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01048, ECO:0000269|PubMed:19629046 |
| Chain | Residue | Details |
| A | GLY10 | |
| B | GLY10 | |
| C | GLY10 | |
| D | GLY10 | |
| E | GLY10 | |
| F | GLY10 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01048 |
| Chain | Residue | Details |
| A | GLY35 | |
| E | ASP56 | |
| F | GLY35 | |
| F | ASP56 | |
| A | ASP56 | |
| B | GLY35 | |
| B | ASP56 | |
| C | GLY35 | |
| C | ASP56 | |
| D | GLY35 | |
| D | ASP56 | |
| E | GLY35 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01048, ECO:0000269|PubMed:19629046, ECO:0000305|PubMed:12446835 |
| Chain | Residue | Details |
| A | ASN120 | |
| B | ASN120 | |
| C | ASN120 | |
| D | ASN120 | |
| E | ASN120 | |
| F | ASN120 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01048, ECO:0000269|PubMed:19629046, ECO:0000269|PubMed:25374115, ECO:0000305 |
| Chain | Residue | Details |
| A | VAL149 | |
| B | VAL149 | |
| C | VAL149 | |
| D | VAL149 | |
| E | VAL149 | |
| F | VAL149 |
