Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005886 | cellular_component | plasma membrane |
A | 0006824 | biological_process | cobalt ion transport |
A | 0009897 | cellular_component | external side of plasma membrane |
A | 0015889 | biological_process | cobalamin transport |
A | 0031419 | molecular_function | cobalamin binding |
A | 0043202 | cellular_component | lysosomal lumen |
A | 0046872 | molecular_function | metal ion binding |
A | 0140355 | molecular_function | cargo receptor ligand activity |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0005886 | cellular_component | plasma membrane |
B | 0006824 | biological_process | cobalt ion transport |
B | 0009897 | cellular_component | external side of plasma membrane |
B | 0015889 | biological_process | cobalamin transport |
B | 0031419 | molecular_function | cobalamin binding |
B | 0043202 | cellular_component | lysosomal lumen |
B | 0046872 | molecular_function | metal ion binding |
B | 0140355 | molecular_function | cargo receptor ligand activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | binding site for residue CNC A 501 |
Chain | Residue |
A | GLY85 |
A | MET270 |
A | GLN273 |
A | SER357 |
A | LEU358 |
A | SER359 |
A | GLY360 |
A | PRO361 |
A | TYR362 |
A | LEU363 |
A | PHE376 |
A | GLN86 |
A | TRP377 |
A | GLN378 |
A | LEU379 |
A | LEU387 |
A | LEU388 |
A | GLY390 |
A | TRP409 |
A | HOH605 |
A | THR134 |
A | TYR137 |
A | GLN138 |
A | ASP176 |
A | ASN224 |
A | TYR226 |
A | SER227 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | SER174 |
A | THR177 |
A | TRP409 |
A | HOH609 |
A | HOH610 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | HIS169 |
A | HIS172 |
A | HIS173 |
A | GLU211 |
A | HOH612 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | GLY372 |
A | GLU373 |
A | GLU375 |
B | GLY372 |
B | GLU375 |
site_id | AC5 |
Number of Residues | 28 |
Details | binding site for residue CNC B 501 |
Chain | Residue |
B | GLY85 |
B | GLN86 |
B | THR134 |
B | TYR137 |
B | GLN138 |
B | ASP176 |
B | ASN224 |
B | TYR226 |
B | SER227 |
B | MET270 |
B | GLN273 |
B | SER357 |
B | LEU358 |
B | SER359 |
B | GLY360 |
B | PRO361 |
B | TYR362 |
B | LEU363 |
B | PHE376 |
B | TRP377 |
B | GLN378 |
B | LEU379 |
B | LEU387 |
B | LEU388 |
B | GLY390 |
B | TRP409 |
B | HOH606 |
B | HOH607 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GOL B 502 |
Chain | Residue |
B | GLN63 |
B | ARG102 |
B | GLY103 |
B | LYS105 |
D | ASP77 |
D | LEU78 |
D | ASP79 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue CA C 201 |
Chain | Residue |
C | TRP150 |
C | ASP153 |
C | HIS155 |
C | ASP157 |
C | ASP163 |
C | GLU164 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue CA C 202 |
Chain | Residue |
C | TRP72 |
C | CYS74 |
C | ASP75 |
C | ASP77 |
C | ASP79 |
C | ASP85 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue CA D 201 |
Chain | Residue |
D | TRP150 |
D | ASP153 |
D | HIS155 |
D | ASP157 |
D | ASP163 |
D | GLU164 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue CA D 202 |
Chain | Residue |
D | ASP85 |
D | TRP72 |
D | ASP75 |
D | ASP77 |
D | ASP79 |
Functional Information from PROSITE/UniProt
site_id | PS00468 |
Number of Residues | 14 |
Details | COBALAMIN_BINDING Eukaryotic cobalamin-binding proteins signature. SVDTAAMAgLAFTC |
Chain | Residue | Details |
A | SER174-CYS187 | |
site_id | PS01209 |
Number of Residues | 27 |
Details | LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CVpltwr.CDrdlDCsdgsDEEcriepC |
Chain | Residue | Details |
C | CYS67-CYS94 | |
C | CYS145-CYS167 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
C | TRP72 | |
C | CYS158 | |
C | GLU164 | |
C | LEU165 | |
D | TRP72 | |
D | ASP75 | |
D | ASP77 | |
D | ASP79 | |
D | ASP85 | |
D | GLU87 | |
D | ARG151 | |
C | ASP75 | |
D | GLY154 | |
D | PRO156 | |
D | CYS158 | |
D | GLU164 | |
D | LEU165 | |
C | ASP77 | |
C | ASP79 | |
C | ASP85 | |
C | GLU87 | |
C | ARG151 | |
C | GLY154 | |
C | PRO156 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
C | CYS127 | |
D | CYS127 | |
A | TRP377 | |
B | THR134 | |
B | ASN224 | |
B | TRP377 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | HIS172 | |
B | HIS172 | |
Chain | Residue | Details |
A | GLN273 | |
B | GLN273 | |