3K3L
Crystal structure of Siderocalin (NGAL, Lipocalin 2) complexed with apo Enterobactin
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 | 10 |
Details | BINDING SITE FOR RESIDUE DBS A 301 |
Chain | Residue |
A | ALA40 |
A | DBH303 |
A | TYR106 |
A | PHE123 |
A | LYS125 |
A | LYS134 |
A | DBH179 |
A | HOH186 |
A | HOH192 |
A | HOH194 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DBH A 303 |
Chain | Residue |
A | TRP79 |
A | DBH179 |
A | HOH194 |
A | DBS301 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DBH A 179 |
Chain | Residue |
A | TYR100 |
A | LYS125 |
A | DBS301 |
A | DBH303 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 3731 |
Chain | Residue |
A | GLN117 |
C | ASN114 |
C | HIS118 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 180 |
Chain | Residue |
A | LYS30 |
A | TYR32 |
A | ASP177 |
A | GLY178 |
A | HOH220 |
C | GLN20 |
C | ASN21 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NA A 181 |
Chain | Residue |
A | THR54 |
A | TYR138 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 182 |
Chain | Residue |
A | THR145 |
A | SER146 |
site_id | AC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE MCK C 179 |
Chain | Residue |
C | ALA40 |
C | ILE41 |
C | TYR52 |
C | LEU70 |
C | TRP79 |
C | TYR106 |
C | PHE123 |
C | LYS125 |
C | TYR132 |
C | PHE133 |
C | LYS134 |
C | HOH186 |
C | HOH199 |
C | HOH224 |
C | HOH243 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 3731 |
Chain | Residue |
C | PRO85 |
C | THR93 |
C | LEU94 |
C | ILE97 |
C | SER105 |
C | TYR106 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL C 180 |
Chain | Residue |
C | LYS59 |
C | GLU60 |
C | ASP61 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL C 181 |
Chain | Residue |
C | LYS50 |
C | ARG72 |
C | LYS73 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 182 |
Chain | Residue |
A | LEU42 |
A | ASN164 |
A | HIS165 |
C | LYS75 |
C | HOH229 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL C 183 |
Chain | Residue |
C | LYS149 |
C | PHE168 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NA C 184 |
Chain | Residue |
C | THR54 |
C | TYR138 |
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 |