4K19
The structure of Human Siderocalin bound to the bacterial siderophore fluvibactin
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 | 1 |
| Details | BINDING SITE FOR RESIDUE FE A 201 |
| Chain | Residue |
| A | 1OD206 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 202 |
| Chain | Residue |
| A | ASN114 |
| A | HIS118 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 203 |
| Chain | Residue |
| A | LEU36 |
| A | TYR52 |
| A | LYS134 |
| A | 1OD206 |
| A | HOH318 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 204 |
| Chain | Residue |
| A | ARG130 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 205 |
| Chain | Residue |
| A | LEU42 |
| A | ASN164 |
| A | HIS165 |
| C | LYS75 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1OD A 206 |
| Chain | Residue |
| A | SER68 |
| A | TRP79 |
| A | ARG81 |
| A | LEU94 |
| A | TYR100 |
| A | LEU103 |
| A | TYR106 |
| A | LYS125 |
| A | TYR132 |
| A | LYS134 |
| A | FE201 |
| A | SO4203 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FE B 201 |
| Chain | Residue |
| B | 1OD202 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 1OD B 202 |
| Chain | Residue |
| B | ALA40 |
| B | TRP79 |
| B | LEU94 |
| B | LEU103 |
| B | TYR106 |
| B | PHE123 |
| B | LYS125 |
| B | LYS134 |
| B | FE201 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FE C 201 |
| Chain | Residue |
| C | 1OD207 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 202 |
| Chain | Residue |
| C | LEU36 |
| C | ILE41 |
| C | TYR52 |
| C | LYS134 |
| C | 1OD207 |
| C | HOH334 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 206 |
| Chain | Residue |
| A | GLN117 |
| C | ASN114 |
| C | HIS118 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1OD C 207 |
| Chain | Residue |
| C | TYR52 |
| C | SER68 |
| C | TRP79 |
| C | ARG81 |
| C | LEU94 |
| C | TYR100 |
| C | LEU103 |
| C | TYR106 |
| C | LYS125 |
| C | LYS134 |
| C | FE201 |
| C | SO4202 |
Functional Information from PROSITE/UniProt
| site_id | PS00213 |
| Number of Residues | 14 |
| Details | LIPOCALIN Lipocalin signature. NFQdnQFQGKWYVV |
| 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 | TYR52 | |
| B | TYR52 | |
| C | TYR52 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0007744|PDB:3CMP |
| Chain | Residue | Details |
| A | TYR106 | |
| A | LYS134 | |
| B | TYR106 | |
| B | LYS134 | |
| C | TYR106 | |
| C | LYS134 |
| 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 |
| A | LYS125 | |
| A | TYR138 | |
| B | LYS125 | |
| B | TYR138 | |
| C | LYS125 | |
| C | TYR138 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:7683678 |
| Chain | Residue | Details |
| A | GLN1 | |
| B | GLN1 | |
| C | GLN1 |
| site_id | SWS_FT_FI5 |
| 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 |
