4YGE
Crystal structure of ERGIC-53/MCFD2, trigonal calcium-bound form 2
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016020 | cellular_component | membrane |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0005793 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment |
B | 0005794 | cellular_component | Golgi apparatus |
B | 0012507 | cellular_component | ER to Golgi transport vesicle membrane |
B | 0015031 | biological_process | protein transport |
B | 0016192 | biological_process | vesicle-mediated transport |
B | 0033116 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment membrane |
B | 0046872 | molecular_function | metal ion binding |
C | 0016020 | cellular_component | membrane |
D | 0005509 | molecular_function | calcium ion binding |
D | 0005515 | molecular_function | protein binding |
D | 0005783 | cellular_component | endoplasmic reticulum |
D | 0005789 | cellular_component | endoplasmic reticulum membrane |
D | 0005793 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment |
D | 0005794 | cellular_component | Golgi apparatus |
D | 0012507 | cellular_component | ER to Golgi transport vesicle membrane |
D | 0015031 | biological_process | protein transport |
D | 0016192 | biological_process | vesicle-mediated transport |
D | 0033116 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment membrane |
D | 0046872 | molecular_function | metal ion binding |
E | 0016020 | cellular_component | membrane |
F | 0005509 | molecular_function | calcium ion binding |
F | 0005515 | molecular_function | protein binding |
F | 0005783 | cellular_component | endoplasmic reticulum |
F | 0005789 | cellular_component | endoplasmic reticulum membrane |
F | 0005793 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment |
F | 0005794 | cellular_component | Golgi apparatus |
F | 0012507 | cellular_component | ER to Golgi transport vesicle membrane |
F | 0015031 | biological_process | protein transport |
F | 0016192 | biological_process | vesicle-mediated transport |
F | 0033116 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment membrane |
F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue CA A 501 |
Chain | Residue |
A | ASP152 |
A | PHE154 |
A | ASN156 |
A | ASP181 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue CA A 502 |
Chain | Residue |
A | ASP155 |
A | ASP157 |
A | ASN161 |
A | ASN162 |
A | ASP181 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue CL A 503 |
Chain | Residue |
A | LYS53 |
A | GLY54 |
A | HIS56 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue CA B 501 |
Chain | Residue |
B | ASP129 |
B | ASN131 |
B | ASP133 |
B | TYR135 |
B | GLU140 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue CA B 502 |
Chain | Residue |
B | ASP81 |
B | ASP83 |
B | ASN85 |
B | LEU87 |
B | GLU92 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue CL C 502 |
Chain | Residue |
C | LYS53 |
C | HIS56 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue CA D 501 |
Chain | Residue |
D | ASP81 |
D | ASP83 |
D | ASN85 |
D | LEU87 |
D | GLU92 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue CA D 502 |
Chain | Residue |
D | ASP129 |
D | ASN131 |
D | ASP133 |
D | TYR135 |
D | GLU140 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue CL E 501 |
Chain | Residue |
E | LYS53 |
E | GLY54 |
E | HIS56 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue CA F 501 |
Chain | Residue |
F | ASP81 |
F | ASP83 |
F | ASN85 |
F | LEU87 |
F | GLU92 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue CA F 502 |
Chain | Residue |
F | ASP129 |
F | ASN131 |
F | ASP133 |
F | TYR135 |
F | GLU140 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DYDGNNLLDglEL |
Chain | Residue | Details |
B | ASP81-LEU93 | |
B | ASP129-PHE141 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 27 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 |
Chain | Residue | Details |
B | ASP81 | |
D | ASP81 | |
D | ASP83 | |
D | ASN85 | |
D | GLU92 | |
D | ASP129 | |
D | ASN131 | |
D | ASP133 | |
D | TYR135 | |
D | GLU140 | |
F | ASP81 | |
B | ASP83 | |
F | ASP83 | |
F | ASN85 | |
F | GLU92 | |
F | ASP129 | |
F | ASN131 | |
F | ASP133 | |
F | TYR135 | |
F | GLU140 | |
B | ASN85 | |
B | GLU92 | |
B | ASP129 | |
B | ASN131 | |
B | ASP133 | |
B | TYR135 | |
B | GLU140 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8K5B3 |
Chain | Residue | Details |
B | SER106 | |
E | PHE154 | |
E | ASN156 | |
E | ASP181 | |
D | SER106 | |
F | SER106 | |
A | ASP181 | |
C | ASP152 | |
C | PHE154 | |
C | ASN156 | |
C | ASP181 | |
E | ASP152 |