4ZHH
Siderocalin-mediated recognition and cellular uptake of actinides
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 |
D | 0005506 | molecular_function | iron ion binding |
D | 0005515 | molecular_function | protein binding |
D | 0005576 | cellular_component | extracellular region |
D | 0005615 | cellular_component | extracellular space |
D | 0006826 | biological_process | iron ion transport |
D | 0006915 | biological_process | apoptotic process |
D | 0015891 | biological_process | siderophore transport |
D | 0031410 | cellular_component | cytoplasmic vesicle |
D | 0035580 | cellular_component | specific granule lumen |
D | 0036094 | molecular_function | small molecule binding |
D | 0042742 | biological_process | defense response to bacterium |
D | 0042802 | molecular_function | identical protein binding |
D | 0045087 | biological_process | innate immune response |
D | 0060205 | cellular_component | cytoplasmic vesicle lumen |
D | 0070062 | cellular_component | extracellular exosome |
D | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
D | 0140315 | molecular_function | iron ion sequestering activity |
D | 1903981 | molecular_function | enterobactin binding |
E | 0005506 | molecular_function | iron ion binding |
E | 0005515 | molecular_function | protein binding |
E | 0005576 | cellular_component | extracellular region |
E | 0005615 | cellular_component | extracellular space |
E | 0006826 | biological_process | iron ion transport |
E | 0006915 | biological_process | apoptotic process |
E | 0015891 | biological_process | siderophore transport |
E | 0031410 | cellular_component | cytoplasmic vesicle |
E | 0035580 | cellular_component | specific granule lumen |
E | 0036094 | molecular_function | small molecule binding |
E | 0042742 | biological_process | defense response to bacterium |
E | 0042802 | molecular_function | identical protein binding |
E | 0045087 | biological_process | innate immune response |
E | 0060205 | cellular_component | cytoplasmic vesicle lumen |
E | 0070062 | cellular_component | extracellular exosome |
E | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
E | 0140315 | molecular_function | iron ion sequestering activity |
E | 1903981 | molecular_function | enterobactin binding |
F | 0005506 | molecular_function | iron ion binding |
F | 0005515 | molecular_function | protein binding |
F | 0005576 | cellular_component | extracellular region |
F | 0005615 | cellular_component | extracellular space |
F | 0006826 | biological_process | iron ion transport |
F | 0006915 | biological_process | apoptotic process |
F | 0015891 | biological_process | siderophore transport |
F | 0031410 | cellular_component | cytoplasmic vesicle |
F | 0035580 | cellular_component | specific granule lumen |
F | 0036094 | molecular_function | small molecule binding |
F | 0042742 | biological_process | defense response to bacterium |
F | 0042802 | molecular_function | identical protein binding |
F | 0045087 | biological_process | innate immune response |
F | 0060205 | cellular_component | cytoplasmic vesicle lumen |
F | 0070062 | cellular_component | extracellular exosome |
F | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
F | 0140315 | molecular_function | iron ion sequestering activity |
F | 1903981 | molecular_function | enterobactin binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | binding site for residue SM A 201 |
Chain | Residue |
A | 4OL202 |
site_id | AC2 |
Number of Residues | 17 |
Details | binding site for residue 4OL A 202 |
Chain | Residue |
A | PHE123 |
A | LYS125 |
A | LYS134 |
A | SM201 |
A | HOH307 |
A | HOH322 |
A | HOH339 |
A | HOH344 |
A | HOH372 |
A | ALA40 |
A | ILE41 |
A | TYR52 |
A | SER68 |
A | TRP79 |
A | ARG81 |
A | TYR100 |
A | TYR106 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 203 |
Chain | Residue |
A | ILE8 |
A | ASN164 |
A | HIS165 |
A | HOH304 |
B | LYS75 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue GOL A 204 |
Chain | Residue |
A | GLN117 |
A | HIS118 |
A | HOH302 |
E | ASN116 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue CL A 205 |
Chain | Residue |
A | THR54 |
A | ARG81 |
A | TYR138 |
A | HOH348 |
A | HOH388 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue SM B 201 |
Chain | Residue |
B | 4OL202 |
site_id | AC7 |
Number of Residues | 16 |
Details | binding site for residue 4OL B 202 |
Chain | Residue |
B | ALA40 |
B | ILE41 |
B | TYR52 |
B | SER68 |
B | LEU70 |
B | TRP79 |
B | TYR100 |
B | TYR106 |
B | LYS125 |
B | LYS134 |
B | SM201 |
B | HOH302 |
B | HOH319 |
B | HOH323 |
B | HOH325 |
B | HOH340 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue SO4 B 203 |
Chain | Residue |
B | ASN114 |
D | GLN117 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue CL B 204 |
Chain | Residue |
B | THR54 |
B | TYR138 |
B | HOH356 |
B | HOH374 |
site_id | AD1 |
Number of Residues | 1 |
Details | binding site for residue SM C 201 |
Chain | Residue |
C | 4OL202 |
site_id | AD2 |
Number of Residues | 18 |
Details | binding site for residue 4OL C 202 |
Chain | Residue |
C | ALA40 |
C | ILE41 |
C | TYR52 |
C | SER68 |
C | TRP79 |
C | ARG81 |
C | TYR100 |
C | TYR106 |
C | LYS125 |
C | LYS134 |
C | SM201 |
C | HOH301 |
C | HOH311 |
C | HOH314 |
C | HOH326 |
C | HOH340 |
C | HOH342 |
D | HOH305 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue SO4 C 203 |
Chain | Residue |
A | GLN117 |
C | ASN114 |
C | HOH303 |
C | HOH306 |
C | HOH322 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue CL C 204 |
Chain | Residue |
C | THR54 |
C | ARG81 |
C | TYR138 |
C | HOH359 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue CL C 205 |
Chain | Residue |
C | SER112 |
C | HIS118 |
site_id | AD6 |
Number of Residues | 1 |
Details | binding site for residue SM D 201 |
Chain | Residue |
D | 4OL202 |
site_id | AD7 |
Number of Residues | 14 |
Details | binding site for residue 4OL D 202 |
Chain | Residue |
D | HOH338 |
D | ALA40 |
D | ILE41 |
D | TYR52 |
D | SER68 |
D | TRP79 |
D | ARG81 |
D | TYR106 |
D | LYS125 |
D | LYS134 |
D | SM201 |
D | HOH304 |
D | HOH307 |
D | HOH319 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue GOL D 203 |
Chain | Residue |
D | ASN114 |
D | HIS118 |
F | ASN116 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue CL D 204 |
Chain | Residue |
D | THR54 |
D | ARG81 |
D | TYR138 |
D | HOH333 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue GOL D 205 |
Chain | Residue |
D | LYS59 |
D | GLU60 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue GOL D 206 |
Chain | Residue |
C | LYS75 |
D | ASN164 |
D | HIS165 |
D | HOH315 |
site_id | AE3 |
Number of Residues | 3 |
Details | binding site for residue CL D 207 |
Chain | Residue |
D | SER112 |
D | HIS118 |
D | ALA119 |
site_id | AE4 |
Number of Residues | 1 |
Details | binding site for residue SM E 201 |
Chain | Residue |
E | 4OL202 |
site_id | AE5 |
Number of Residues | 15 |
Details | binding site for residue 4OL E 202 |
Chain | Residue |
E | ALA40 |
E | ILE41 |
E | TYR52 |
E | SER68 |
E | LEU70 |
E | TRP79 |
E | TYR106 |
E | PHE123 |
E | LYS125 |
E | LYS134 |
E | SM201 |
E | HOH301 |
E | HOH310 |
E | HOH321 |
E | HOH334 |
site_id | AE6 |
Number of Residues | 4 |
Details | binding site for residue SO4 E 203 |
Chain | Residue |
D | ARG154 |
E | THR145 |
E | SER146 |
E | HOH335 |
site_id | AE7 |
Number of Residues | 3 |
Details | binding site for residue CL E 204 |
Chain | Residue |
E | THR54 |
E | ARG81 |
E | TYR138 |
site_id | AE8 |
Number of Residues | 1 |
Details | binding site for residue GOL E 205 |
Chain | Residue |
E | LYS73 |
site_id | AE9 |
Number of Residues | 1 |
Details | binding site for residue SM F 201 |
Chain | Residue |
F | 4OL202 |
site_id | AF1 |
Number of Residues | 17 |
Details | binding site for residue 4OL F 202 |
Chain | Residue |
F | ALA40 |
F | ILE41 |
F | TYR52 |
F | SER68 |
F | LEU70 |
F | TRP79 |
F | ARG81 |
F | TYR106 |
F | LYS125 |
F | LYS134 |
F | SM201 |
F | HOH303 |
F | HOH313 |
F | HOH314 |
F | HOH316 |
F | HOH349 |
F | HOH356 |
site_id | AF2 |
Number of Residues | 4 |
Details | binding site for residue SO4 F 203 |
Chain | Residue |
E | LYS75 |
F | PRO162 |
F | ASN164 |
F | HIS165 |
site_id | AF3 |
Number of Residues | 3 |
Details | binding site for residue CL F 204 |
Chain | Residue |
F | THR54 |
F | ARG81 |
F | 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 | 6 |
Details | BINDING: BINDING => ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U |
Chain | Residue | Details |
A | TYR52 | |
B | TYR52 | |
C | TYR52 | |
D | TYR52 | |
E | TYR52 | |
F | TYR52 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0007744|PDB:3CMP |
Chain | Residue | Details |
A | TYR106 | |
E | LYS134 | |
F | TYR106 | |
F | LYS134 | |
A | LYS134 | |
B | TYR106 | |
B | LYS134 | |
C | TYR106 | |
C | LYS134 | |
D | TYR106 | |
D | LYS134 | |
E | TYR106 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15642259, ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U |
Chain | Residue | Details |
A | LYS125 | |
E | TYR138 | |
F | LYS125 | |
F | TYR138 | |
A | TYR138 | |
B | LYS125 | |
B | TYR138 | |
C | LYS125 | |
C | TYR138 | |
D | LYS125 | |
D | TYR138 | |
E | LYS125 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:7683678 |
Chain | Residue | Details |
A | GLN1 | |
B | GLN1 | |
C | GLN1 | |
D | GLN1 | |
E | GLN1 | |
F | GLN1 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
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 | |
D | ASN65 | |
E | ASN65 | |
F | ASN65 |