3FW4
Crystal structure of Siderocalin (NGAL, Lipocalin 2) complexed with Ferric Catechol
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 | 2 |
Details | BINDING SITE FOR RESIDUE FE A 179 |
Chain | Residue |
A | TYR106 |
A | CAQ180 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CAQ A 180 |
Chain | Residue |
A | TYR106 |
A | PHE123 |
A | LYS125 |
A | TYR132 |
A | LYS134 |
A | FE179 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 183 |
Chain | Residue |
A | ARG81 |
A | TYR138 |
A | THR54 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 184 |
Chain | Residue |
A | LYS142 |
A | GLU143 |
A | ASP173 |
C | GLN20 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 185 |
Chain | Residue |
A | ASN96 |
A | SER99 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 186 |
Chain | Residue |
A | THR145 |
A | SER146 |
A | GLU147 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 188 |
Chain | Residue |
A | LYS125 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 190 |
Chain | Residue |
A | HIS118 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FE B 179 |
Chain | Residue |
B | ARG81 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 180 |
Chain | Residue |
B | TYR52 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 181 |
Chain | Residue |
B | TRP79 |
B | ARG81 |
B | TYR100 |
site_id | BC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FE C 179 |
Chain | Residue |
C | CAQ180 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CAQ C 180 |
Chain | Residue |
C | PHE123 |
C | LYS125 |
C | LYS134 |
C | FE179 |
C | GOL188 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NA C 181 |
Chain | Residue |
A | GLN117 |
C | HOH272 |
site_id | BC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NA C 182 |
Chain | Residue |
A | LYS75 |
site_id | BC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NA C 183 |
Chain | Residue |
C | SER146 |
site_id | BC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NA C 184 |
Chain | Residue |
C | HOH266 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL C 185 |
Chain | Residue |
C | TRP79 |
C | ARG81 |
site_id | CC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL C 186 |
Chain | Residue |
C | PHE22 |
C | ASP24 |
C | PRO85 |
C | GLN88 |
C | PRO89 |
C | GLY90 |
C | GLU91 |
C | PHE92 |
C | HOH211 |
C | HOH300 |
C | HOH320 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 187 |
Chain | Residue |
C | PRO85 |
C | LEU94 |
C | ILE97 |
C | TYR106 |
C | HOH326 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 188 |
Chain | Residue |
C | ALA40 |
C | LYS125 |
C | TYR132 |
C | CAQ180 |
C | HOH297 |
site_id | CC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 189 |
Chain | Residue |
C | LEU18 |
C | GLN19 |
C | GLN20 |
C | VAL111 |
C | SER112 |
C | HOH239 |
C | HOH259 |
site_id | CC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE GOL C 190 |
Chain | Residue |
C | ARG130 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL C 3731 |
Chain | Residue |
C | LYS59 |
C | GLU60 |
C | ASP61 |
site_id | CC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL C 191 |
Chain | Residue |
B | GLN23 |
C | ASN116 |
C | ARG140 |
C | HOH279 |
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 |