6QMU
A tetrahedral boronic acid diester formed by a non-natural amino acid in the ligand pocket of an engineered lipocalin
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residues ZCQ A 201 and 7N8 A 36 |
| Chain | Residue |
| A | GLY35 |
| A | ILE135 |
| A | PHE152 |
| A | VAL167 |
| A | TRP181 |
| A | SER182 |
| A | HOH318 |
| A | HOH332 |
| A | HOH334 |
| A | ALA37 |
| A | ILE41 |
| A | PHE52 |
| A | SER68 |
| A | TRP79 |
| A | ARG81 |
| A | TRP125 |
| A | ASN134 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residues ZCQ A 201 and 7N8 A 36 |
| Chain | Residue |
| A | GLY35 |
| A | ALA37 |
| A | ILE41 |
| A | PHE52 |
| A | SER68 |
| A | TRP79 |
| A | ARG81 |
| A | TRP125 |
| A | ASN134 |
| A | ILE135 |
| A | PHE152 |
| A | VAL167 |
| A | TRP181 |
| A | SER182 |
| A | HOH318 |
| A | HOH332 |
| A | HOH334 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for Di-peptide GLY B 35 and 7N8 B 36 |
| Chain | Residue |
| B | VAL33 |
| B | VAL34 |
| B | ALA37 |
| B | ILE41 |
| B | TRP125 |
| B | ASN134 |
| B | ILE135 |
| B | THR136 |
| B | LEU137 |
| B | PHE152 |
| B | VAL167 |
| B | SER182 |
| B | ZCQ201 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide 7N8 B 36 and ALA B 37 |
| Chain | Residue |
| B | GLY35 |
| B | GLY38 |
| B | ILE41 |
| B | TRP125 |
| B | ASN134 |
| B | ILE135 |
| B | PHE152 |
| B | SER156 |
| B | HIS165 |
| B | VAL167 |
| B | SER182 |
| B | ZCQ201 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residues ZCQ B 201 and 7N8 B 36 |
| Chain | Residue |
| B | GLY35 |
| B | ALA37 |
| B | ILE41 |
| B | LEU70 |
| B | TRP79 |
| B | TRP125 |
| B | ASN134 |
| B | ILE135 |
| B | PHE152 |
| B | VAL167 |
| B | TRP181 |
| B | SER182 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residues ZCQ B 201 and 7N8 B 36 |
| Chain | Residue |
| B | GLY35 |
| B | ALA37 |
| B | ILE41 |
| B | LEU70 |
| B | TRP79 |
| B | TRP125 |
| B | ASN134 |
| B | ILE135 |
| B | PHE152 |
| B | VAL167 |
| B | TRP181 |
| B | SER182 |
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 | 2 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U |
| Chain | Residue | Details |
| A | PHE52 | |
| B | PHE52 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0007744|PDB:3CMP |
| Chain | Residue | Details |
| A | TYR106 | |
| A | ASN134 | |
| B | TYR106 | |
| B | ASN134 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15642259, ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U |
| Chain | Residue | Details |
| B | TRP125 | |
| B | TYR138 | |
| A | TRP125 | |
| A | TYR138 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:7683678 |
| Chain | Residue | Details |
| A | GLN1 | |
| B | GLN1 |
| 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 | |
| B | ASN65 |
