6SUA
Structure of the high affinity engineered lipocalin C1B12 in complex with the mouse CD98 heavy chain ectodomain
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 | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006865 | biological_process | amino acid transport |
| 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 |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0006865 | biological_process | amino acid transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 201 |
| Chain | Residue |
| A | PRO12 |
| A | LEU13 |
| A | LYS124 |
| A | GLU131 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 601 |
| Chain | Residue |
| B | SER465 |
| B | ARG467 |
| B | HOH722 |
| B | THR303 |
| B | THR305 |
| B | ARG308 |
| B | ARG463 |
| B | ASP464 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 602 |
| Chain | Residue |
| B | TRP111 |
| B | LYS114 |
| B | LYS150 |
| B | HIS196 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 603 |
| Chain | Residue |
| A | LYS98 |
| B | ASP341 |
| B | HIS342 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 604 |
| Chain | Residue |
| B | ASP243 |
| B | GLY245 |
| B | LYS246 |
| B | THR274 |
| B | GLU275 |
| B | GLN331 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 605 |
| Chain | Residue |
| B | ARG467 |
| B | SER468 |
| B | ARG470 |
| B | HOH742 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 201 |
| Chain | Residue |
| C | PRO12 |
| C | LEU13 |
| C | LYS124 |
| C | GLU131 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 601 |
| Chain | Residue |
| D | THR303 |
| D | THR305 |
| D | ARG308 |
| D | HOH741 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 602 |
| Chain | Residue |
| D | GLU426 |
| D | ARG427 |
| D | SER428 |
| D | ASN453 |
| D | GLU454 |
| D | TYR456 |
| D | HOH704 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 603 |
| Chain | Residue |
| D | TRP111 |
| D | LYS114 |
| D | LYS150 |
| D | HIS196 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 604 |
| Chain | Residue |
| D | PRO340 |
| D | ASP341 |
| D | HIS342 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 605 |
| Chain | Residue |
| D | ARG467 |
| D | SER468 |
| D | ARG470 |
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 | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P08195 |
| Chain | Residue | Details |
| B | SER300 | |
| B | SER302 | |
| B | SER420 | |
| D | SER300 | |
| D | SER302 | |
| D | SER420 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770 |
| Chain | Residue | Details |
| B | ASN166 | |
| B | ASN259 | |
| B | ASN385 | |
| B | ASN399 | |
| D | ASN166 | |
| D | ASN259 | |
| D | ASN385 | |
| D | ASN399 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| B | ASN263 | |
| B | ASN301 | |
| B | ASN509 | |
| D | ASN263 | |
| D | ASN301 | |
| D | ASN509 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P08195 |
| Chain | Residue | Details |
| B | ASN318 | |
| D | ASN318 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| 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 | |
| C | ASN65 |
