6GR0
Petrobactin-binding engineered lipocalin in complex with gallium-petrobactin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0006826 | biological_process | iron ion transport |
| A | 0006915 | biological_process | apoptotic process |
| A | 0015891 | biological_process | siderophore transport |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| A | 0035580 | cellular_component | specific granule lumen |
| A | 0036094 | molecular_function | small molecule binding |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045087 | biological_process | innate immune response |
| A | 0060205 | cellular_component | cytoplasmic vesicle lumen |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
| A | 0140315 | molecular_function | iron ion sequestering activity |
| A | 1903981 | molecular_function | enterobactin binding |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0006826 | biological_process | iron ion transport |
| B | 0006915 | biological_process | apoptotic process |
| B | 0015891 | biological_process | siderophore transport |
| B | 0031410 | cellular_component | cytoplasmic vesicle |
| B | 0035580 | cellular_component | specific granule lumen |
| B | 0036094 | molecular_function | small molecule binding |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0045087 | biological_process | innate immune response |
| B | 0060205 | cellular_component | cytoplasmic vesicle lumen |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
| B | 0140315 | molecular_function | iron ion sequestering activity |
| B | 1903981 | molecular_function | enterobactin binding |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005615 | cellular_component | extracellular space |
| C | 0006826 | biological_process | iron ion transport |
| C | 0006915 | biological_process | apoptotic process |
| C | 0015891 | biological_process | siderophore transport |
| C | 0031410 | cellular_component | cytoplasmic vesicle |
| C | 0035580 | cellular_component | specific granule lumen |
| C | 0036094 | molecular_function | small molecule binding |
| C | 0042742 | biological_process | defense response to bacterium |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0045087 | biological_process | innate immune response |
| C | 0060205 | cellular_component | cytoplasmic vesicle lumen |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
| C | 0140315 | molecular_function | iron ion sequestering activity |
| C | 1903981 | molecular_function | enterobactin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue F8W A 201 |
| Chain | Residue |
| A | PHE36 |
| A | LYS132 |
| A | TRP134 |
| A | THR136 |
| A | GA202 |
| A | HOH315 |
| A | HOH316 |
| A | HOH317 |
| A | HOH319 |
| A | HOH327 |
| A | HOH331 |
| A | ILE52 |
| A | HOH335 |
| A | HOH337 |
| A | HOH342 |
| A | ASN68 |
| A | ARG79 |
| A | ILE80 |
| A | LYS81 |
| A | ARG100 |
| A | MET103 |
| A | TYR106 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue GA A 202 |
| Chain | Residue |
| A | F8W201 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | binding site for residue F8W B 201 |
| Chain | Residue |
| B | PHE36 |
| B | ILE52 |
| B | ASN68 |
| B | ARG79 |
| B | ILE80 |
| B | LYS81 |
| B | ARG100 |
| B | MET103 |
| B | TYR106 |
| B | LYS132 |
| B | TRP134 |
| B | THR136 |
| B | GA202 |
| B | HOH311 |
| B | HOH315 |
| B | HOH325 |
| B | HOH328 |
| B | HOH334 |
| B | HOH339 |
| B | HOH340 |
| B | HOH349 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue GA B 202 |
| Chain | Residue |
| B | F8W201 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue F8W B 203 |
| Chain | Residue |
| A | LYS75 |
| A | LYS75 |
| A | THR77 |
| A | TYR78 |
| A | ARG79 |
| A | HOH307 |
| B | GLU143 |
| B | GLU143 |
| B | PHE168 |
| B | F8W204 |
| B | GA205 |
| B | GA205 |
| B | GA206 |
| B | HOH320 |
| B | HOH327 |
| B | HOH327 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | binding site for residue F8W B 204 |
| Chain | Residue |
| A | GLU74 |
| A | LYS75 |
| B | GLU74 |
| B | LYS75 |
| B | GLU143 |
| B | PRO171 |
| B | F8W203 |
| B | GA206 |
| B | HOH303 |
| B | HOH305 |
| B | HOH336 |
| B | HOH351 |
| C | GLU143 |
| C | VAL170 |
| C | PRO171 |
| C | F8W203 |
| C | GA204 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue GA B 205 |
| Chain | Residue |
| A | LYS75 |
| A | HOH301 |
| B | GLU143 |
| B | F8W203 |
| B | F8W203 |
| B | GA206 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue GA B 206 |
| Chain | Residue |
| A | HOH301 |
| B | GLU143 |
| B | F8W203 |
| B | F8W204 |
| B | GA205 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | binding site for residue F8W C 201 |
| Chain | Residue |
| C | THR136 |
| C | GA202 |
| C | HOH306 |
| C | HOH308 |
| C | HOH318 |
| C | HOH321 |
| C | HOH328 |
| C | PHE36 |
| C | ILE52 |
| C | ASN68 |
| C | ILE80 |
| C | LYS81 |
| C | ARG100 |
| C | MET103 |
| C | TYR106 |
| C | LYS132 |
| C | TRP134 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue GA C 202 |
| Chain | Residue |
| C | F8W201 |
| site_id | AD2 |
| Number of Residues | 19 |
| Details | binding site for residue F8W C 203 |
| Chain | Residue |
| B | LYS75 |
| B | THR77 |
| B | TYR78 |
| B | ARG79 |
| B | F8W204 |
| B | HOH317 |
| B | HOH317 |
| B | HOH326 |
| C | GLU143 |
| C | GLU143 |
| C | LYS149 |
| C | PHE168 |
| C | PRO169 |
| C | PRO171 |
| C | GA204 |
| C | GA205 |
| C | GA205 |
| C | HOH309 |
| C | HOH337 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue GA C 204 |
| Chain | Residue |
| B | F8W204 |
| B | HOH301 |
| C | GLU143 |
| C | F8W203 |
| C | GA205 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue GA C 205 |
| Chain | Residue |
| B | HOH301 |
| C | GLU143 |
| C | F8W203 |
| C | F8W203 |
| C | GA204 |
Functional Information from PROSITE/UniProt
| site_id | PS00213 |
| Number of Residues | 14 |
| Details | LIPOCALIN Lipocalin signature. NFQdnQFHGKWYVV |
| Chain | Residue | Details |
| A | ASN21-VAL34 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U |
| Chain | Residue | Details |
| A | ILE52 | |
| B | ILE52 | |
| C | ILE52 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0007744|PDB:3CMP |
| Chain | Residue | Details |
| A | TYR106 | |
| A | TRP134 | |
| B | TYR106 | |
| B | TRP134 | |
| C | TYR106 | |
| C | TRP134 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15642259, ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U |
| Chain | Residue | Details |
| B | TYR138 | |
| C | THR125 | |
| C | TYR138 | |
| A | THR125 | |
| A | TYR138 | |
| B | THR125 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10684642, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7683678, ECO:0007744|PDB:1DFV, ECO:0007744|PDB:1QQS |
| Chain | Residue | Details |
| A | ASN65 | |
| B | ASN65 | |
| C | ASN65 |
